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PDBsum entry 1gof

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protein ligands metals links
Oxidoreductase(oxygen(a)) PDB id
1gof
Jmol
Contents
Protein chain
639 a.a. *
Ligands
ACY ×2
Metals
_CU
_NA
Waters ×316
* Residue conservation analysis
PDB id:
1gof
Name: Oxidoreductase(oxygen(a))
Title: Novel thioether bond revealed by a 1.7 angstroms crystal str galactose oxidase
Structure: Galactose oxidase. Chain: a. Engineered: yes
Source: Hypomyces rosellus. Organism_taxid: 5132
Resolution:
1.70Å     R-factor:   0.177    
Authors: N.Ito,S.E.V.Phillips,P.F.Knowles
Key ref: N.Ito et al. (1991). Novel thioether bond revealed by a 1.7 A crystal structure of galactose oxidase. Nature, 350, 87-90. PubMed id: 2002850 DOI: 10.1038/350087a0
Date:
30-Sep-93     Release date:   31-Jan-94    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam  
P0CS93  (GAOA_GIBZA) -  Galactose oxidase
Seq:
Struc:
 
Seq:
Struc:
680 a.a.
639 a.a.
Key:    Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.1.1.3.9  - Galactose oxidase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: D-galactose + O2 = D-galacto-hexodialdose + H2O2
D-galactose
+ O(2)
= D-galacto-hexodialdose
+ H(2)O(2)
      Cofactor: Copper
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   1 term 
  Biological process     cell adhesion   2 terms 
  Biochemical function     oxidoreductase activity     3 terms  

 

 
    reference    
 
 
DOI no: 10.1038/350087a0 Nature 350:87-90 (1991)
PubMed id: 2002850  
 
 
Novel thioether bond revealed by a 1.7 A crystal structure of galactose oxidase.
N.Ito, S.E.Phillips, C.Stevens, Z.B.Ogel, M.J.McPherson, J.N.Keen, K.D.Yadav, P.F.Knowles.
 
  ABSTRACT  
 
Galactose oxidase is an extracellular enzyme secreted by the fungus Dactylium dendroides. It is monomeric, with a relative molecular mass of 68,000, catalyses the stereospecific oxidation of a broad range of primary alcohol substrates and possesses a unique mononuclear copper site essential for catalysing a two-electron transfer reaction during the oxidation of primary alcohols to corresponding aldehydes. Recent evidence arguing against a Cu(III)-Cu(I) couple implies the existence of a second redox-active site proposed to involve pyrroloquinoline quinone or a tyrosine radical. We now report the crystal structure of galactose oxidase at 1.7 A resolution. This reveals a unique structural feature at the copper site with a novel thioether bond linking Cys 228 and Tyr 272 in a stacking interaction with Trp 290. We propose that these molecular components stabilize the protein free-radical species essential for catalysis and thus provide a 'built-in' secondary cofactor. This feature may represent a new mechanism for mediating electron transfer in metalloenzymes in the absence of exogenous cofactors.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21283844 A.Mijovilovich, S.Hamman, F.Thomas, F.M.de Groot, and B.M.Weckhuysen (2011).
Protonation of the oxygen axial ligand in galactose oxidase model compounds as seen with high resolution X-ray emission experiments and FEFF simulations.
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21055949 H.J.Kang, and E.N.Baker (2011).
Intramolecular isopeptide bonds: protein crosslinks built for stress?
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20195658 M.H.Stipanuk, C.R.Simmons, P.Andrew Karplus, and J.E.Dominy (2011).
Thiol dioxygenases: unique families of cupin proteins.
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20936199 V.L.Davidson (2011).
Generation of protein-derived redox cofactors by posttranslational modification.
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21077113 F.Aparecido Cordeiro, C.Bertechini Faria, and I.Parra Barbosa-Tessmann (2010).
Identification of new galactose oxidase genes in Fusarium spp.
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20820605 H.Arora, C.Philouze, O.Jarjayes, and F.Thomas (2010).
Co(II), Ni(II), Cu(II) and Zn(II) complexes of a bipyridine bis-phenol conjugate: generation and properties of coordinated radical species.
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20372697 J.A.Worrall, and E.Vijgenboom (2010).
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20836876 O.Spadiut, L.Olsson, and H.Brumer (2010).
A comparative summary of expression systems for the recombinant production of galactose oxidase.
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20939100 S.Kalkhof, S.Haehn, M.Paulsson, N.Smyth, J.Meiler, and A.Sinz (2010).
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Engineering enzyme specificity using computational design of a defined-sequence library.
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19156277 F.Michel, S.Hamman, C.Philouze, C.P.Del Valle, E.Saint-Aman, and F.Thomas (2009).
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19290629 K.J.Humphreys, L.M.Mirica, Y.Wang, and J.P.Klinman (2009).
Galactose oxidase as a model for reactivity at a copper superoxide center.
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19107892 S.K.Alamsetti, S.Mannam, P.Mutupandi, and G.Sekar (2009).
Galactose oxidase model: biomimetic enantiomer-differentiating oxidation of alcohols by a chiral copper complex.
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Metal complexes of amino acids and amino acid side chain groups. Structures and properties.
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18478142 A.John, M.M.Shaikh, and P.Ghosh (2008).
Structural and functional mimic of galactose oxidase by a copper complex of a sterically demanding [N2O2] ligand.
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18057969 D.Rokhsana, D.M.Dooley, and R.K.Szilagyi (2008).
Systematic development of computational models for the catalytic site in galactose oxidase: impact of outer-sphere residues on the geometric and electronic structures.
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18063573 E.Severi, A.Müller, J.R.Potts, A.Leech, D.Williamson, K.S.Wilson, and G.H.Thomas (2008).
Sialic acid mutarotation is catalyzed by the Escherichia coli beta-propeller protein YjhT.
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PDB code: 2uvk
18330849 F.Escalettes, and N.J.Turner (2008).
Directed evolution of galactose oxidase: generation of enantioselective secondary alcohol oxidases.
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18308719 J.E.Dominy, J.Hwang, S.Guo, L.L.Hirschberger, S.Zhang, and M.H.Stipanuk (2008).
Synthesis of amino acid cofactor in cysteine dioxygenase is regulated by substrate and represents a novel post-translational regulation of activity.
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18384150 K.S.Aragão, M.Satre, A.Imberty, and A.Varrot (2008).
Structure determination of Discoidin II from Dictyostelium discoideum and carbohydrate binding properties of the lectin domain.
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PDB codes: 2vm9 2vmc 2vmd 2vme
18800132 L.Que, and W.B.Tolman (2008).
Biologically inspired oxidation catalysis.
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18771294 M.S.Rogers, R.Hurtado-Guerrero, S.J.Firbank, M.A.Halcrow, D.M.Dooley, S.E.Phillips, P.F.Knowles, and M.J.McPherson (2008).
Cross-link formation of the cysteine 228-tyrosine 272 catalytic cofactor of galactose oxidase does not require dioxygen.
  Biochemistry, 47, 10428-10439.
PDB codes: 2vz1 2vz3
18985252 M.Stylianou, C.Drouza, Z.Viskadourakis, J.Giapintzakis, and A.D.Keramidas (2008).
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17680689 T.J.Stevens, and M.Paoli (2008).
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18512952 Y.K.Lee, M.M.Whittaker, and J.W.Whittaker (2008).
The electronic structure of the Cys-Tyr(*) free radical in galactose oxidase determined by EPR spectroscopy.
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17786587 G.N.Phillips, B.G.Fox, J.L.Markley, B.F.Volkman, E.Bae, E.Bitto, C.A.Bingman, R.O.Frederick, J.G.McCoy, B.L.Lytle, B.S.Pierce, J.Song, and S.N.Twigger (2007).
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The stacking tryptophan of galactose oxidase: a second-coordination sphere residue that has profound effects on tyrosyl radical behavior and enzyme catalysis.
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PDB codes: 2eib 2eic 2eid 2eie
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17024269 F.Michel, S.Hamman, F.Thomas, C.Philouze, I.Gautier-Luneau, and J.L.Pierre (2006).
Galactose Oxidase models: 19F NMR as a powerful tool to study the solution chemistry of tripodal ligands in the presence of copper(II).
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16492780 J.G.McCoy, L.J.Bailey, E.Bitto, C.A.Bingman, D.J.Aceti, B.G.Fox, and G.N.Phillips (2006).
Structure and mechanism of mouse cysteine dioxygenase.
  Proc Natl Acad Sci U S A, 103, 3084-3089.
PDB code: 2atf
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Genome sequence and global gene expression of Q54, a new phage species linking the 936 and c2 phage species of Lactococcus lactis.
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16770835 M.A.Hossain, F.Thomas, S.Hamman, E.Saint-Aman, D.Boturyn, P.Dumy, and J.L.Pierre (2006).
Cyclodecapeptides to mimic the radical site of tyrosyl-containing proteins.
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16810650 O.Rotthaus, F.Thomas, O.Jarjayes, C.Philouze, E.Saint-Aman, and J.L.Pierre (2006).
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16218875 A.Berkessel, M.Dousset, S.Bulat, and K.Glaubitz (2005).
Combinatorial approaches to functional models for galactose oxidase.
  Biol Chem, 386, 1035-1041.  
15578222 B.Leuthner, C.Aichinger, E.Oehmen, E.Koopmann, O.Müller, P.Müller, R.Kahmann, M.Bölker, and P.H.Schreier (2005).
A H2O2-producing glyoxal oxidase is required for filamentous growth and pathogenicity in Ustilago maydis.
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15580644 F.Michel, S.Torelli, F.Thomas, C.Duboc, C.Philouze, C.Belle, S.Hamman, E.Saint-Aman, and J.L.Pierre (2005).
An unprecedented bridging phenoxyl radical in dicopper(II) complexes: evidence for an s=3/2 spin state.
  Angew Chem Int Ed Engl, 44, 438-441.  
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Structure of Ca2+ release channel at 14 A resolution.
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Iron(III) activation hits a [4 + 4] macrocycle.
  Dalton Trans, (), 429-432.  
15741346 J.Song, R.C.Tyler, R.L.Wrobel, R.O.Frederick, F.C.Vojtek, W.B.Jeon, M.S.Lee, and J.L.Markley (2005).
Solution structure of At3g04780.1-des15, an Arabidopsis thaliana ortholog of the C-terminal domain of human thioredoxin-like protein.
  Protein Sci, 14, 1059-1063.
PDB code: 1xoy
15696544 M.D.Swain, and D.E.Benson (2005).
Geometric preferences of crosslinked protein-derived cofactors reveal a high propensity for near-sequence pairs.
  Proteins, 59, 64-71.  
15678420 M.Groll, M.Bochtler, H.Brandstetter, T.Clausen, and R.Huber (2005).
Molecular machines for protein degradation.
  Chembiochem, 6, 222-256.  
16218874 P.Chaudhuri, K.Wieghardt, T.Weyhermüller, T.K.Paine, S.Mukherjee, and C.Mukherjee (2005).
Biomimetic metal-radical reactivity: aerial oxidation of alcohols, amines, aminophenols and catechols catalyzed by transition metal complexes.
  Biol Chem, 386, 1023-1033.  
15840564 R.A.Ghiladi, G.M.Knudsen, K.F.Medzihradszky, and P.R.Ortiz de Montellano (2005).
The Met-Tyr-Trp cross-link in Mycobacterium tuberculosis catalase-peroxidase (KatG): autocatalytic formation and effect on enzyme catalysis and spectroscopic properties.
  J Biol Chem, 280, 22651-22663.  
15917234 R.Schnell, T.Sandalova, U.Hellman, Y.Lindqvist, and G.Schneider (2005).
Siroheme- and [Fe4-S4]-dependent NirA from Mycobacterium tuberculosis is a sulfite reductase with a covalent Cys-Tyr bond in the active site.
  J Biol Chem, 280, 27319-27328.
PDB codes: 1zj8 1zj9
15854824 S.Shleev, J.Tkac, A.Christenson, T.Ruzgas, A.I.Yaropolov, J.W.Whittaker, and L.Gorton (2005).
Direct electron transfer between copper-containing proteins and electrodes.
  Biosens Bioelectron, 20, 2517-2554.  
16030250 T.Harashima, and J.Heitman (2005).
Galpha subunit Gpa2 recruits kelch repeat subunits that inhibit receptor-G protein coupling during cAMP-induced dimorphic transitions in Saccharomyces cerevisiae.
  Mol Biol Cell, 16, 4557-4571.  
15465324 G.R.Vasta, H.Ahmed, and E.W.Odom (2004).
Structural and functional diversity of lectin repertoires in invertebrates, protochordates and ectothermic vertebrates.
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15317589 H.Danielsson Thorell, N.H.Beyer, N.H.Heegaard, M.Ohman, and T.Nilsson (2004).
Comparison of native and recombinant chlorite dismutase from Ideonella dechloratans.
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15299013 R.M.Vanacore, S.Shanmugasundararaj, D.B.Friedman, O.Bondar, B.G.Hudson, and M.Sundaramoorthy (2004).
The alpha1.alpha2 network of collagen IV. Reinforced stabilization of the noncollagenous domain-1 by noncovalent forces and the absence of Met-Lys cross-links.
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PDB codes: 1t60 1t61
15239055 S.E.Deacon, K.Mahmoud, R.K.Spooner, S.J.Firbank, P.F.Knowles, S.E.Phillips, and M.J.McPherson (2004).
Enhanced fructose oxidase activity in a galactose oxidase variant.
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PDB code: 2jkx
15583386 X.Li, D.Zhang, M.Hannink, and L.J.Beamer (2004).
Crystallization and initial crystallographic analysis of the Kelch domain from human Keap1.
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15475350 X.Li, D.Zhang, M.Hannink, and L.J.Beamer (2004).
Crystal structure of the Kelch domain of human Keap1.
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Crystal structure of the human neuropilin-1 b1 domain.
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PDB code: 1kex
12672814 M.M.Whittaker, and J.W.Whittaker (2003).
Cu(I)-dependent biogenesis of the galactose oxidase redox cofactor.
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Crystal structure of fungal lectin: six-bladed beta-propeller fold and novel fucose recognition mode for Aleuria aurantia lectin.
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PDB code: 1ofz
12429700 A.M.Hudson, and L.Cooley (2002).
Understanding the function of actin-binding proteins through genetic analysis of Drosophila oogenesis.
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12429703 C.M.Hull, and J.Heitman (2002).
Genetics of Cryptococcus neoformans.
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Structural basis for the processive protein degradation by tricorn protease.
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12091873 M.A.Bianchet, E.W.Odom, G.R.Vasta, and L.M.Amzel (2002).
A novel fucose recognition fold involved in innate immunity.
  Nat Struct Biol, 9, 628-634.
PDB code: 1k12
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X-ray snapshots of quinone cofactor biogenesis in bacterial copper amine oxidase.
  Nat Struct Biol, 9, 591-596.
PDB codes: 1ivu 1ivv 1ivw 1ivx
11854274 U.Coskun, G.Grüber, M.H.Koch, J.Godovac-Zimmermann, T.Lemker, and V.Müller (2002).
Cross-talk in the A1-ATPase from Methanosarcina mazei Go1 due to nucleotide binding.
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11937049 Z.Jawad, and M.Paoli (2002).
Novel sequences propel familiar folds.
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12404359 E.I.Solomon, P.Chen, M.Metz, S.K.Lee, and A.E.Palmer (2001).
Oxygen Binding, Activation, and Reduction to Water by Copper Proteins.
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Crystal structure of the tricorn protease reveals a protein disassembly line.
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PDB code: 1k32
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How many ways to craft a cofactor?
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11698675 L.Xie, and W.A.van der Donk (2001).
Homemade cofactors: self-processing in galactose oxidase.
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Chemically Modified Amino Acids in Copper Proteins That Bind or Activate Dioxygen The author acknowledges the Royal Society (London) for a University Research Fellowship.
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The solution structure of PapGII from uropathogenic Escherichia coli and its recognition of glycolipid receptors.
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Catalytic control of redox reactivities of coenzyme analogs by metal ions.
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11698678 S.J.Firbank, M.S.Rogers, C.M.Wilmot, D.M.Dooley, M.A.Halcrow, P.F.Knowles, M.J.McPherson, and S.E.Phillips (2001).
Crystal structure of the precursor of galactose oxidase: an unusual self-processing enzyme.
  Proc Natl Acad Sci U S A, 98, 12932-12937.
PDB code: 1k3i
10736169 B.Schwartz, J.E.Dove, and J.P.Klinman (2000).
Kinetic analysis of oxygen utilization during cofactor biogenesis in a copper-containing amine oxidase from yeast.
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10891502 C.A.Gomez, L.M.Ptaszek, A.Villa, F.Bozzi, C.Sobacchi, E.G.Brooks, L.D.Notarangelo, E.Spanopoulou, Z.Q.Pan, P.Vezzoni, P.Cortes, and S.Santagata (2000).
Mutations in conserved regions of the predicted RAG2 kelch repeats block initiation of V(D)J recombination and result in primary immunodeficiencies.
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10847687 D.C.Nelson, J.Lasswell, L.E.Rogg, M.A.Cohen, and B.Bartel (2000).
FKF1, a clock-controlled gene that regulates the transition to flowering in Arabidopsis.
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A groovy new structure.
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10642183 M.J.Colaneri, J.Vitali, and J.Peisach (2000).
Electron spin-echo envelope modulation study of multicrystalline Cu(2+)-insulin: effects of Cd(2+) on the nuclear quadrupole interaction of the Cu(2+)-coordinated imidazole remote nitrogen.
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Novel cofactors via post-translational modifications of enzyme active sites.
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Buried charged surface in proteins.
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PDB code: 1f9c
10742191 V.Mahadevan, R.K.Gebbink, and T.D.Stack (2000).
Biomimetic modeling of copper oxidase reactivity.
  Curr Opin Chem Biol, 4, 228-234.  
10556574 A.Durmus, C.Eicken, F.Spener, and B.Krebs (1999).
Cloning and comparative protein modeling of two purple acid phosphatase isozymes from sweet potatoes (Ipomoea batatas).
  Biochim Biophys Acta, 1434, 202-209.  
10612596 B.E.Turner, and B.P.Branchaud (1999).
Probing the radical mechanism of galactose oxidase using an ultrafast radical probe.
  Bioorg Med Chem Lett, 9, 3341-3346.  
10607672 C.Eicken, B.Krebs, and J.C.Sacchettini (1999).
Catechol oxidase - structure and activity.
  Curr Opin Struct Biol, 9, 677-683.  
10556561 D.A.Svistunenko, A.Rob, A.Ball, J.Torres, M.C.Symons, M.T.Wilson, and C.E.Cooper (1999).
The electron paramagnetic resonance characterisation of a copper-containing extracellular peroxidase from Thermomonospora fusca BD25.
  Biochim Biophys Acta, 1434, 74-85.  
10226046 H.C.Liang, M.Dahan, and K.D.Karlin (1999).
Dioxygen-activating bio-inorganic model complexes.
  Curr Opin Chem Biol, 3, 168-175.  
10228146 H.G.Beisel, S.Kawabata, S.Iwanaga, R.Huber, and W.Bode (1999).
Tachylectin-2: crystal structure of a specific GlcNAc/GalNAc-binding lectin involved in the innate immunity host defense of the Japanese horseshoe crab Tachypleus tridentatus.
  EMBO J, 18, 2313-2322.
PDB code: 1tl2
10194323 J.L.Johnson, D.C.Norcross, P.Arosio, R.B.Frankel, and G.D.Watt (1999).
Redox reactivity of animal apoferritins and apoheteropolymers assembled from recombinant heavy and light human chain ferritins.
  Biochemistry, 38, 4089-4096.  
10226045 M.A.McGuirl, and D.M.Dooley (1999).
Copper-containing oxidases.
  Curr Opin Chem Biol, 3, 138-144.  
10607670 V.Fülöp, and D.T.Jones (1999).
Beta propellers: structural rigidity and functional diversity.
  Curr Opin Struct Biol, 9, 715-721.  
10601271 X.Huang, M.P.Cuajungco, C.S.Atwood, M.A.Hartshorn, J.D.Tyndall, G.R.Hanson, K.C.Stokes, M.Leopold, G.Multhaup, L.E.Goldstein, R.C.Scarpa, A.J.Saunders, J.Lim, R.D.Moir, C.Glabe, E.F.Bowden, C.L.Masters, D.P.Fairlie, R.E.Tanzi, and A.I.Bush (1999).
Cu(II) potentiation of alzheimer abeta neurotoxicity. Correlation with cell-free hydrogen peroxide production and metal reduction.
  J Biol Chem, 274, 37111-37116.  
9560195 C.Oxvig, and T.A.Springer (1998).
Experimental support for a beta-propeller domain in integrin alpha-subunits and a calcium binding site on its lower surface.
  Proc Natl Acad Sci U S A, 95, 4870-4875.
PDB code: 1a8x
9694833 D.P.Molloy, A.E.Milner, I.K.Yakub, G.Chinnadurai, P.H.Gallimore, and R.J.Grand (1998).
Structural determinants present in the C-terminal binding protein binding site of adenovirus early region 1A proteins.
  J Biol Chem, 273, 20867-20876.  
9693734 M.Karpefors, P.Adelroth, A.Aagaard, H.Sigurdson, M.Svensson Ek, and P.Brzezinski (1998).
Electron-proton interactions in terminal oxidases.
  Biochim Biophys Acta, 1365, 159-169.  
9622494 M.M.Whittaker, D.P.Ballou, and J.W.Whittaker (1998).
Kinetic isotope effects as probes of the mechanism of galactose oxidase.
  Biochemistry, 37, 8426-8436.  
  9742080 O.Denisenko, M.Shnyreva, H.Suzuki, and K.Bomsztyk (1998).
Point mutations in the WD40 domain of Eed block its interaction with Ezh2.
  Mol Cell Biol, 18, 5634-5642.  
9566959 T.A.Kim, J.Lim, S.Ota, S.Raja, R.Rogers, B.Rivnay, H.Avraham, and S.Avraham (1998).
NRP/B, a novel nuclear matrix protein, associates with p110(RB) and is involved in neuronal differentiation.
  J Cell Biol, 141, 553-566.  
9846879 T.Klabunde, C.Eicken, J.C.Sacchettini, and B.Krebs (1998).
Crystal structure of a plant catechol oxidase containing a dicopper center.
  Nat Struct Biol, 5, 1084-1090.
PDB codes: 1bt1 1bt2 1bt3 1bug
  9696811 T.Wolff, R.E.O'Neill, and P.Palese (1998).
NS1-Binding protein (NS1-BP): a novel human protein that interacts with the influenza A virus nonstructural NS1 protein is relocalized in the nuclei of infected cells.
  J Virol, 72, 7170-7180.  
9438841 Y.Wang, J.L.DuBois, B.Hedman, K.O.Hodgson, and T.D.Stack (1998).
Catalytic galactose oxidase models: biomimetic Cu(II)-phenoxyl-radical reactivity.
  Science, 279, 537-540.  
9241431 C.Chothia, T.Hubbard, S.Brenner, H.Barns, and A.Murzin (1997).
Protein folds in the all-beta and all-alpha classes.
  Annu Rev Biophys Biomol Struct, 26, 597-627.  
9331415 D.Nurizzo, M.C.Silvestrini, M.Mathieu, F.Cutruzzolà, D.Bourgeois, V.Fülöp, J.Hajdu, M.Brunori, M.Tegoni, and C.Cambillau (1997).
N-terminal arm exchange is observed in the 2.15 A crystal structure of oxidized nitrite reductase from Pseudomonas aeruginosa.
  Structure, 5, 1157-1171.
PDB code: 1nir
9166791 J.M.Matthews, L.D.Ward, A.Hammacher, R.S.Norton, and R.J.Simpson (1997).
Roles of histidine 31 and tryptophan 34 in the structure, self-association, and folding of murine interleukin-6.
  Biochemistry, 36, 6187-6196.  
  9343430 J.Ng, R.Li, K.Morgan, and J.Simon (1997).
Evolutionary conservation and predicted structure of the Drosophila extra sex combs repressor protein.
  Mol Cell Biol, 17, 6663-6672.  
  9094665 K.A.Simmen, A.Newell, M.Robinson, J.S.Mills, G.Canning, R.Handa, K.Parkes, N.Borkakoti, and R.Jupp (1997).
Protein interactions in the herpes simplex virus type 1 VP16-induced complex: VP16 peptide inhibition and mutational analysis of host cell factor requirements.
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8990162 T.A.Springer (1997).
Folding of the N-terminal, ligand-binding region of integrin alpha-subunits into a beta-propeller domain.
  Proc Natl Acad Sci U S A, 94, 65-72.  
  9278056 T.F.Smith, L.Lo Conte, J.Bienkowska, C.Gaitatzes, R.G.Rogers, and R.Lathrop (1997).
Current limitations to protein threading approaches.
  J Comput Biol, 4, 217-225.  
9367957 U.Ermler, W.Grabarse, S.Shima, M.Goubeaud, and R.K.Thauer (1997).
Crystal structure of methyl-coenzyme M reductase: the key enzyme of biological methane formation.
  Science, 278, 1457-1462.
PDB code: 1mro
8889170 C.Ma, and B.A.Barry (1996).
Electron paramagnetic resonance characterization of tyrosine radical, M+, in site-directed mutants of photosystem II(t).
  Biophys J, 71, 1961-1972.  
8851656 D.E.Coleman, and S.R.Sprang (1996).
How G proteins work: a continuing story.
  Trends Biochem Sci, 21, 41-44.  
8805541 F.Mancia, N.H.Keep, A.Nakagawa, P.F.Leadlay, S.McSweeney, B.Rasmussen, P.Bösecke, O.Diat, and P.R.Evans (1996).
How coenzyme B12 radicals are generated: the crystal structure of methylmalonyl-coenzyme A mutase at 2 A resolution.
  Structure, 4, 339-350.
PDB code: 1req
8679595 M.E.Anderson, and P.A.Lindahl (1996).
Spectroscopic states of the CO oxidation/CO2 reduction active site of carbon monoxide dehydrogenase and mechanistic implications.
  Biochemistry, 35, 8371-8380.  
8916929 R.M.Wachter, and B.P.Branchaud (1996).
Thiols as mechanistic probes for catalysis by the free radical enzyme galactose oxidase.
  Biochemistry, 35, 14425-14435.  
8527681 G.A.Landrum, C.A.Ekberg, and J.W.Whittaker (1995).
A ligand field model for MCD spectra of biological cupric complexes.
  Biophys J, 69, 674-689.  
8521505 M.A.Wall, D.E.Coleman, E.Lee, J.A.Iñiguez-Lluhi, B.A.Posner, A.G.Gilman, and S.R.Sprang (1995).
The structure of the G protein heterotrimer Gi alpha 1 beta 1 gamma 2.
  Cell, 83, 1047-1058.
PDB codes: 1gg2 1gp2
  7787112 M.F.Schmid, J.Jakana, P.Matsudaira, and W.Chiu (1995).
Three-dimensional structure of the acrosomal filament of Limulus sperm by 400 kV electron cryomicroscopy.
  Biophys J, 68, 8S.  
8591022 M.Fontecave, and H.Eklund (1995).
Copper amine oxidase: a novel use for a tyrosine.
  Structure, 3, 1127-1129.  
8591028 M.R.Parsons, M.A.Convery, C.M.Wilmot, K.D.Yadav, V.Blakeley, A.S.Corner, S.E.Phillips, M.J.McPherson, and P.F.Knowles (1995).
Crystal structure of a quinoenzyme: copper amine oxidase of Escherichia coli at 2 A resolution.
  Structure, 3, 1171-1184.
PDB code: 1oac
8536678 R.J.Williams (1995).
Energised (entatic) states of groups and of secondary structures in proteins and metalloproteins.
  Eur J Biochem, 234, 363-381.  
7876189 S.L.Edwards, V.L.Davidson, Y.L.Hyun, and P.T.Wingfield (1995).
Spectroscopic evidence for a common electron transfer pathway for two tryptophan tryptophylquinone enzymes.
  J Biol Chem, 270, 4293-4298.  
8502724 B.A.Barry (1993).
The role of redox-active amino acids in the photosynthetic water-oxidizing complex.
  Photochem Photobiol, 57, 179-188.  
8081735 C.Chothia, and A.G.Murzin (1993).
New folds for all-beta proteins.
  Structure, 1, 217-222.  
8268003 J.Harder (1993).
Ribonucleotide reductases and their occurrence in microorganisms: a link to the RNA/DNA transition.
  FEMS Microbiol Rev, 12, 273-292.  
8386015 M.M.Whittaker, and J.W.Whittaker (1993).
Ligand interactions with galactose oxidase: mechanistic insights.
  Biophys J, 64, 762-772.  
8346264 P.J.Kersten, and D.Cullen (1993).
Cloning and characterization of cDNA encoding glyoxal oxidase, a H2O2-producing enzyme from the lignin-degrading basidiomycete Phanerochaete chrysosporium.
  Proc Natl Acad Sci U S A, 90, 7411-7413.  
8291091 R.T.Dean, S.Gieseg, and M.J.Davies (1993).
Reactive species and their accumulation on radical-damaged proteins.
  Trends Biochem Sci, 18, 437-441.  
  8366046 X.Zhang, J.H.Fuller, and W.S.McIntire (1993).
Cloning, sequencing, expression, and regulation of the structural gene for the copper/topa quinone-containing methylamine oxidase from Arthrobacter strain P1, a gram-positive facultative methylotroph.
  J Bacteriol, 175, 5617-5627.  
1368439 J.A.Tainer, V.A.Roberts, and E.D.Getzoff (1992).
Protein metal-binding sites.
  Curr Opin Biotechnol, 3, 378-387.  
1367679 J.A.Tainer, V.A.Roberts, and E.D.Getzoff (1991).
Metal-binding sites in proteins.
  Curr Opin Biotechnol, 2, 582-591.  
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