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PDBsum entry 1ah7

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protein metals links
Hydrolase PDB id
1ah7
Jmol
Contents
Protein chain
245 a.a. *
Metals
_ZN ×3
Waters ×232
* Residue conservation analysis
PDB id:
1ah7
Name: Hydrolase
Title: PhospholipasE C from bacillus cereus
Structure: PhospholipasE C. Chain: a. Synonym: phosphatidylcholine-hydrolyzing phospholipasE C. Ec: 3.1.4.3
Source: Bacillus cereus. Organism_taxid: 1396
Biol. unit: Monomer (from PDB file)
Resolution:
1.50Å     R-factor:   0.203     R-free:   0.231
Authors: R.Greaves
Key ref: E.Hough et al. (1989). High-resolution (1.5 A) crystal structure of phospholipase C from Bacillus cereus. Nature, 338, 357-360. PubMed id: 2493587
Date:
14-Apr-97     Release date:   10-Dec-97    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P09598  (PHLC_BACCE) -  Phospholipase C
Seq:
Struc:
283 a.a.
245 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.1.4.3  - Phospholipase C.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: A phosphatidylcholine + H2O = 1,2-diacyl-sn-glycerol + phosphocholine
phosphatidylcholine
+ H(2)O
= 1,2-diacyl-sn-glycerol
+ phosphocholine
      Cofactor: Zinc
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     metabolic process   3 terms 
  Biochemical function     hydrolase activity     6 terms  

 

 
    reference    
 
 
Nature 338:357-360 (1989)
PubMed id: 2493587  
 
 
High-resolution (1.5 A) crystal structure of phospholipase C from Bacillus cereus.
E.Hough, L.K.Hansen, B.Birknes, K.Jynge, S.Hansen, A.Hordvik, C.Little, E.Dodson, Z.Derewenda.
 
  ABSTRACT  
 
Both the phosphatidylinositol-hydrolysing and the phosphatidylcholine-hydrolysing phospholipases C have been implicated in the generation of second messengers in mammalian cells. The phosphatidylcholine-hydrolysing phospholipase C (PLC) from Bacillus cereus, a monomeric protein containing 245 amino-acid residues, is similar to some of the corresponding mammalian proteins. This, together with the fact that the bacterial enzyme can mimic the action of mammalian PLC in causing, for example, enhanced prostaglandin biosynthesis, suggests that B. cereus PLC can be used as a model for the hitherto poorly characterized mammalian PLCs. We report here the three-dimensional structure of B. cereus PLC at 1.5 A resolution. The enzyme is an all-helix protein belonging to a novel structural class and contains, at least in the crystalline state, three Zn2+ in the active site. We also present preliminary results from a study at 1.9 A resolution of the complex between PLC and inorganic phosphate (Pi) which indicate that the substrate binds directly to the metal ions.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21310143 M.Kim, Y.S.Park, D.S.Shin, J.Kim, B.G.Kim, and Y.S.Lee (2011).
Antibody-free peptide substrate screening of serine/threonine kinase (protein kinase A) with a biotinylated detection probe.
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20854710 W.Yang (2011).
Nucleases: diversity of structure, function and mechanism.
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20135039 D.R.Edwards, W.Y.Tsang, A.A.Neverov, and R.S.Brown (2010).
On the question of stepwise vs. concerted cleavage of RNA models promoted by a synthetic dinuclear Zn(II) complex in methanol: implementation of a noncleavable phosphonate probe.
  Org Biomol Chem, 8, 822-827.  
20879990 E.R.Slepkov, A.Pavinski Bitar, and H.Marquis (2010).
Differentiation of propeptide residues regulating the compartmentalization, maturation and activity of the broad-range phospholipase C of Listeria monocytogenes.
  Biochem J, 432, 557-563.  
20683537 M.Jarenmark, E.Csapó, J.Singh, S.Wöckel, E.Farkas, F.Meyer, M.Haukka, and E.Nordlander (2010).
Unsymmetrical dizinc complexes as models for the active sites of phosphohydrolases.
  Dalton Trans, 39, 8183-8194.  
20564046 M.Kim, D.S.Shin, J.Kim, and Y.S.Lee (2010).
Substrate screening of protein kinases: Detection methods and combinatorial peptide libraries.
  Biopolymers, 94, 753-762.  
19727456 D.Anselmo, E.C.Escudero-Adán, J.Benet-Buchholz, and A.W.Kleij (2009).
Assembly of unusual Zn-cluster compounds based on pyridinealcohol platforms.
  Dalton Trans, (), 7368-7373.  
19272175 S.L.Wu, C.C.Li, J.C.Chen, Y.J.Chen, C.T.Lin, T.Y.Ho, and C.Y.Hsiang (2009).
Mutagenesis identifies the critical amino acid residues of human endonuclease G involved in catalysis, magnesium coordination, and substrate specificity.
  J Biomed Sci, 16, 6.  
18688403 A.B.Curtiss, M.Bera, G.T.Musie, and D.R.Powell (2008).
Synthesis and characterization of mono- and micro6-sulfato hexanuclear zinc complexes of a new symmetric dinucleating ligand.
  Dalton Trans, (), 2717-2724.  
18648861 A.Tamilselvi, and G.Mugesh (2008).
Zinc and antibiotic resistance: metallo-beta-lactamases and their synthetic analogues.
  J Biol Inorg Chem, 13, 1039-1053.  
18408731 E.D.Garcin, D.J.Hosfield, S.A.Desai, B.J.Haas, M.Björas, R.P.Cunningham, and J.A.Tainer (2008).
DNA apurinic-apyrimidinic site binding and excision by endonuclease IV.
  Nat Struct Mol Biol, 15, 515-522.
PDB codes: 2nq9 2nqh 2nqj
18697748 K.Syson, C.Tomlinson, B.R.Chapados, J.R.Sayers, J.A.Tainer, N.H.Williams, and J.A.Grasby (2008).
Three metal ions participate in the reaction catalyzed by t5 flap endonuclease.
  J Biol Chem, 283, 28741-28746.  
17324372 A.P.Benfield, N.M.Goodey, L.T.Phillips, and S.F.Martin (2007).
Structural studies examining the substrate specificity profiles of PC-PLC(Bc) protein variants.
  Arch Biochem Biophys, 460, 41-47.
PDB codes: 2ffz 2fgn 2huc
17893790 R.Mitra, M.W.Peters, and M.J.Scott (2007).
Synthesis and reactivity of a C3-symmetric trinuclear zinc(II) hydroxide catalyst efficient at phosphate diester transesterification.
  Dalton Trans, (), 3924-3935.  
16538247 F.H.Zelder, R.Salvio, and J.Rebek (2006).
A synthetic receptor for phosphocholine esters.
  Chem Commun (Camb), (), 1280-1282.  
16892359 J.M.Rondeau, F.Bitsch, E.Bourgier, M.Geiser, R.Hemmig, M.Kroemer, S.Lehmann, P.Ramage, S.Rieffel, A.Strauss, J.R.Green, and W.Jahnke (2006).
Structural basis for the exceptional in vivo efficacy of bisphosphonate drugs.
  ChemMedChem, 1, 267-273.
PDB codes: 2f7m 2f89 2f8c 2f8z 2f92 2f94 2f9k
17191935 P.R.Reddy, P.Manjula, and S.K.Mohan (2005).
Novel peptide-based copper(II) complexes for total hydrolytic cleavage of DNA.
  Chem Biodivers, 2, 1338-1350.  
17192010 P.R.Reddy, S.K.Mohan, and K.S.Rao (2005).
Ternary zinc(II)-dipeptide complexes for the hydrolytic cleavage of DNA at physiological pH.
  Chem Biodivers, 2, 672-683.  
15805506 P.S.Yeung, N.Zagorski, and H.Marquis (2005).
The metalloprotease of Listeria monocytogenes controls cell wall translocation of the broad-range phospholipase C.
  J Bacteriol, 187, 2601-2608.  
15930776 Y.Wang, and N.Okabe (2005).
Crystal structures and spectroscopic properties of zinc(II) ternary complexes of vitamin L, H' and their isomer m-aminobenzoic acid with bipyridine.
  Chem Pharm Bull (Tokyo), 53, 645-652.  
14978036 S.W.Nelson, R.B.Honzatko, and H.J.Fromm (2004).
Origin of cooperativity in the activation of fructose-1,6-bisphosphatase by Mg2+.
  J Biol Chem, 279, 18481-18487.  
12661000 A.Teplyakov, G.Obmolova, P.P.Khil, A.J.Howard, R.D.Camerini-Otero, and G.L.Gilliland (2003).
Crystal structure of the Escherichia coli YcdX protein reveals a trinuclear zinc active site.
  Proteins, 51, 315-318.
PDB codes: 1m65 1m68
12632471 M.Elstner, Q.Cui, P.Munih, E.Kaxiras, T.Frauenheim, and M.Karplus (2003).
Modeling zinc in biomolecules with the self consistent charge-density functional tight binding (SCC-DFTB) method: applications to structural and energetic analysis.
  J Comput Chem, 24, 565-581.  
12030321 A.González-Roura, J.Casas, and A.Llebaria (2002).
Synthesis and phospholipase C inhibitory activity of D609 diastereomers.
  Lipids, 37, 401-406.  
12029081 A.Vogel, O.Schilling, M.Niecke, J.Bettmer, and W.Meyer-Klaucke (2002).
ElaC encodes a novel binuclear zinc phosphodiesterase.
  J Biol Chem, 277, 29078-29085.  
12410824 M.J.Stonehouse, A.Cota-Gomez, S.K.Parker, W.E.Martin, J.A.Hankin, R.C.Murphy, W.Chen, K.B.Lim, M.Hackett, A.I.Vasil, and M.L.Vasil (2002).
A novel class of microbial phosphocholine-specific phospholipases C.
  Mol Microbiol, 46, 661-676.  
11551776 M.S.Weiss, M.Brandl, J.Sühnel, D.Pal, and R.Hilgenfeld (2001).
More hydrogen bonds for the (structural) biologist.
  Trends Biochem Sci, 26, 521-523.  
11333021 V.Tereshko, S.T.Wallace, N.Usman, F.E.Wincott, and M.Egli (2001).
X-ray crystallographic observation of "in-line" and "adjacent" conformations in a bulged self-cleaving RNA/DNA hybrid.
  RNA, 7, 405-420.
PDB codes: 1i2x 1i2y
10948154 D.J.Beecher, T.W.Olsen, E.B.Somers, and A.C.Wong (2000).
Evidence for contribution of tripartite hemolysin BL, phosphatidylcholine-preferring phospholipase C, and collagenase to virulence of Bacillus cereus endophthalmitis.
  Infect Immun, 68, 5269-5276.  
10873862 I.Leiros, F.Secundo, C.Zambonelli, S.Servi, and E.Hough (2000).
The first crystal structure of a phospholipase D.
  Structure, 8, 655-667.
PDB code: 1f0i
  10850800 K.M.Holtz, B.Stec, J.K.Myers, S.M.Antonelli, T.S.Widlanski, and E.R.Kantrowitz (2000).
Alternate modes of binding in two crystal structures of alkaline phosphatase-inhibitor complexes.
  Protein Sci, 9, 907-915.
PDB codes: 1ew8 1ew9
10727235 S.F.Martin, B.C.Follows, P.J.Hergenrother, and B.K.Trotter (2000).
The choline binding site of phospholipase C (Bacillus cereus): insights into substrate specificity.
  Biochemistry, 39, 3410-3415.  
10924156 S.H.Francis, I.V.Turko, K.A.Grimes, and J.D.Corbin (2000).
Histidine-607 and histidine-643 provide important interactions for metal support of catalysis in phosphodiesterase-5.
  Biochemistry, 39, 9591-9596.  
10458614 D.J.Hosfield, Y.Guan, B.J.Haas, R.P.Cunningham, and J.A.Tainer (1999).
Structure of the DNA repair enzyme endonuclease IV and its DNA complex: double-nucleotide flipping at abasic sites and three-metal-ion catalysis.
  Cell, 98, 397-408.
PDB codes: 1qtw 1qum
10194360 S.F.Martin, and P.J.Hergenrother (1999).
Catalytic cycle of the phosphatidylcholine-preferring phospholipase C from Bacillus cereus. Solvent viscosity, deuterium isotope effects, and proton inventory studies.
  Biochemistry, 38, 4403-4408.  
9521750 C.A.Tan, and M.F.Roberts (1998).
Engineering of the nonspecific phospholipase C from Bacillus cereus: replacement of glutamic acid-4 by alanine results in loss of interfacial catalysis and enhanced phosphomonoesterase activity.
  Biochemistry, 37, 4275-4279.  
9699639 C.E.Naylor, J.T.Eaton, A.Howells, N.Justin, D.S.Moss, R.W.Titball, and A.K.Basak (1998).
Structure of the key toxin in gas gangrene.
  Nat Struct Biol, 5, 738-746.
PDB code: 1ca1
9667939 J.E.Coleman (1998).
Zinc enzymes.
  Curr Opin Chem Biol, 2, 222-234.  
9891801 J.I.Rood (1998).
Virulence genes of Clostridium perfringens.
  Annu Rev Microbiol, 52, 333-360.  
9733734 M.Flores-Díaz, A.Alape-Girón, R.W.Titball, M.Moos, I.Guillouard, S.Cole, A.M.Howells, C.von Eichel-Streiber, I.Florin, and M.Thelestam (1998).
UDP-glucose deficiency causes hypersensitivity to the cytotoxic effect of Clostridium perfringens phospholipase C.
  J Biol Chem, 273, 24433-24438.  
9831527 R.Jelinek, S.Okada, S.Norvez, and D.Charych (1998).
Interfacial catalysis by phospholipases at conjugated lipid vesicles: colorimetric detection and NMR spectroscopy.
  Chem Biol, 5, 619-629.  
9548962 S.F.Martin, and P.J.Hergenrother (1998).
General base catalysis by the phosphatidylcholine-preferring phospholipase C from Bacillus cereus: the role of Glu4 and Asp55.
  Biochemistry, 37, 5755-5760.  
9871566 S.F.Martin, and P.J.Hergenrother (1998).
Enzymatic synthesis of a modified phospholipid and its evaluation as a substrate for B. cereus phospholipase C.
  Bioorg Med Chem Lett, 8, 593-596.  
9660788 S.L.Schissel, G.A.Keesler, E.H.Schuchman, K.J.Williams, and I.Tabas (1998).
The cellular trafficking and zinc dependence of secretory and lysosomal sphingomyelinase, two products of the acid sphingomyelinase gene.
  J Biol Chem, 273, 18250-18259.  
9730812 S.M.Fabiane, M.K.Sohi, T.Wan, D.J.Payne, J.H.Bateson, T.Mitchell, and B.J.Sutton (1998).
Crystal structure of the zinc-dependent beta-lactamase from Bacillus cereus at 1.9 A resolution: binuclear active site with features of a mononuclear enzyme.
  Biochemistry, 37, 12404-12411.
PDB code: 1bc2
  9746585 W.R.Zückert, H.Marquis, and H.Goldfine (1998).
Modulation of enzymatic activity and biological function of Listeria monocytogenes broad-range phospholipase C by amino acid substitutions and by replacement with the Bacillus cereus ortholog.
  Infect Immun, 66, 4823-4831.  
9699620 Z.S.Derewenda, and T.W.Martin (1998).
Structure of the gangrene alpha-toxin: the beauty in the beast.
  Nat Struct Biol, 5, 659-662.  
9782777 D.Suck (1997).
DNA recognition by structure-selective nucleases.
  Biopolymers, 44, 405-421.  
9279125 D.da Graça Thrige, J.R.Buur, and F.S.Jørgensen (1997).
Substrate binding and catalytic mechanism in phospholipase C from Bacillus cereus: a molecular mechanics and molecular dynamics study.
  Biopolymers, 42, 319-336.  
9218451 G.Bujacz, J.Alexandratos, A.Wlodawer, G.Merkel, M.Andrake, R.A.Katz, and A.M.Skalka (1997).
Binding of different divalent cations to the active site of avian sarcoma virus integrase and their effects on enzymatic activity.
  J Biol Chem, 272, 18161-18168.
PDB codes: 1vsh 1vsi 1vsj
9100023 G.Chen, T.Edwards, V.M.D'souza, and R.C.Holz (1997).
Mechanistic studies on the aminopeptidase from Aeromonas proteolytica: a two-metal ion mechanism for peptide hydrolysis.
  Biochemistry, 36, 4278-4286.  
  9234819 M.Nagahama, T.Nakayama, K.Michiue, and J.Sakurai (1997).
Site-specific mutagenesis of Clostridium perfringens alpha-toxin: replacement of Asp-56, Asp-130, or Glu-152 causes loss of enzymatic and hemolytic activities.
  Infect Immun, 65, 3489-3492.  
9054547 Y.Chen, X.Li, and P.Gegenheimer (1997).
Ribonuclease P catalysis requires Mg2+ coordinated to the pro-RP oxygen of the scissile bond.
  Biochemistry, 36, 2425-2438.  
8811285 C.Moser, H.P.Roth, and M.Kirchgessner (1996).
Influence of alimentary zinc deficiency on the concentration of the second messengers D-myo-inositol-1,4,5-trisphosphate (IP3) and s,n-1,2-diacylglycerol (DAG) in testes and brain of force-fed rats.
  Biol Trace Elem Res, 52, 281-291.  
8862751 H.P.Roth, C.Moser, and M.Kirchgessner (1996).
Subcellular distribution of protein kinase C (pKC) in erythrocytes and concentration of D-myo-inositol-1,4,5-trisphosphate (IP3) in platelets and monocytes of force-fed zinc-deficient rats.
  Biol Trace Elem Res, 53, 225-234.  
  8698464 I.Guillouard, T.Garnier, and S.T.Cole (1996).
Use of site-directed mutagenesis to probe structure-function relationships of alpha-toxin from Clostridium perfringens.
  Infect Immun, 64, 2440-2444.  
8961562 M.Nagahama, K.Michiue, and J.Sakurai (1996).
Production and purification of Clostridium perfringens alpha-toxin using a protein-hyperproducing strain, Bacillus brevis 47.
  FEMS Microbiol Lett, 145, 239-243.  
8805566 N.O.Concha, B.A.Rasmussen, K.Bush, and O.Herzberg (1996).
Crystal structure of the wide-spectrum binuclear zinc beta-lactamase from Bacteroides fragilis.
  Structure, 4, 823-836.
PDB code: 1znb
8841144 S.F.Martin, M.R.Spaller, and P.J.Hergenrother (1996).
Expression and site-directed mutagenesis of the phosphatidylcholine-preferring phospholipase C of Bacillus cereus: probing the role of the active site Glu146.
  Biochemistry, 35, 12970-12977.  
  8976554 Y.Matsuo, A.Yamada, K.Tsukamoto, H.Tamura, H.Ikezawa, H.Nakamura, and K.Nishikawa (1996).
A distant evolutionary relationship between bacterial sphingomyelinase and mammalian DNase I.
  Protein Sci, 5, 2459-2467.  
  7664726 D.W.Heinz, M.Ryan, T.L.Bullock, and O.H.Griffith (1995).
Crystal structure of the phosphatidylinositol-specific phospholipase C from Bacillus cereus in complex with myo-inositol.
  EMBO J, 14, 3855-3863.
PDB codes: 1ptd 1ptg
  7628431 E.M.Schad, I.Zaitseva, V.N.Zaitsev, M.Dohlsten, T.Kalland, P.M.Schlievert, D.H.Ohlendorf, and L.A.Svensson (1995).
Crystal structure of the superantigen staphylococcal enterotoxin type A.
  EMBO J, 14, 3292-3301.
PDB code: 1esf
7816101 J.Grimes, A.K.Basak, P.Roy, and D.Stuart (1995).
The crystal structure of bluetongue virus VP7.
  Nature, 373, 167-170.
PDB code: 1bvp
  8522524 K.Tsutsui, J.Minami, O.Matsushita, S.Katayama, Y.Taniguchi, S.Nakamura, M.Nishioka, and A.Okabe (1995).
Phylogenetic analysis of phospholipase C genes from Clostridium perfringens types A to E and Clostridium novyi.
  J Bacteriol, 177, 7164-7170.  
  7868589 M.Nagahama, Y.Okagawa, T.Nakayama, E.Nishioka, and J.Sakurai (1995).
Site-directed mutagenesis of histidine residues in Clostridium perfringens alpha-toxin.
  J Bacteriol, 177, 1179-1185.  
8087555 B.Chevrier, C.Schalk, H.D'Orchymont, J.M.Rondeau, D.Moras, and C.Tarnus (1994).
Crystal structure of Aeromonas proteolytica aminopeptidase: a prototypical member of the co-catalytic zinc enzyme family.
  Structure, 2, 283-291.
PDB code: 1amp
7925409 I.Crevel, S.U, A.Carne, and M.Katan (1994).
Purification and properties of zinc-metallophospholipase C from Pseudomonas fluorescens.
  Eur J Biochem, 224, 845-852.  
8076805 M.Nagahama, H.Iida, E.Nishioka, K.Okamoto, and J.Sakurai (1994).
Roles of the carboxy-terminal region of Clostridium perfringens alpha toxin.
  FEMS Microbiol Lett, 120, 297-301.  
  8264633 T.Johansen, G.Bjørkøy, A.Overvatn, M.T.Diaz-Meco, T.Traavik, and J.Moscat (1994).
NIH 3T3 cells stably transfected with the gene encoding phosphatidylcholine-hydrolyzing phospholipase C from Bacillus cereus acquire a transformed phenotype.
  Mol Cell Biol, 14, 646-654.  
  7703848 T.T.Tibbitts, X.Xu, and E.R.Kantrowitz (1994).
Kinetics and crystal structure of a mutant Escherichia coli alkaline phosphatase (Asp-369-->Asn): a mechanism involving one zinc per active site.
  Protein Sci, 3, 2005-2014.
PDB code: 1alh
7849238 Y.P.Tu, and H.Xu (1994).
Zn2+ inhibits the anion transport activity of band 3 by binding to its cytoplasmic tail.
  Biosci Rep, 14, 159-169.  
8464881 B.L.Vallee, and D.S.Auld (1993).
Cocatalytic zinc motifs in enzyme catalysis.
  Proc Natl Acad Sci U S A, 90, 2715-2718.  
  7693592 M.Y.Zhang, A.Lövgren, M.G.Low, and R.Landén (1993).
Characterization of an avirulent pleiotropic mutant of the insect pathogen Bacillus thuringiensis: reduced expression of flagellin and phospholipases.
  Infect Immun, 61, 4947-4954.  
  8336671 R.W.Titball (1993).
Bacterial phospholipases C.
  Microbiol Rev, 57, 347-366.  
8341661 T.A.Steitz, and J.A.Steitz (1993).
A general two-metal-ion mechanism for catalytic RNA.
  Proc Natl Acad Sci U S A, 90, 6498-6502.  
8386017 T.L.Bullock, M.Ryan, S.L.Kim, S.J.Remington, and O.H.Griffith (1993).
Crystallization of phosphatidylinositol-specific phospholipase C from Bacillus cereus.
  Biophys J, 64, 784-791.  
  1309513 J.A.Vazquez-Boland, C.Kocks, S.Dramsi, H.Ohayon, C.Geoffroy, J.Mengaud, and P.Cossart (1992).
Nucleotide sequence of the lecithinase operon of Listeria monocytogenes and possible role of lecithinase in cell-to-cell spread.
  Infect Immun, 60, 219-230.  
1412693 J.B.Vincent, M.W.Crowder, and B.A.Averill (1992).
Hydrolysis of phosphate monoesters: a biological problem with multiple chemical solutions.
  Trends Biochem Sci, 17, 105-110.  
1579567 J.R.Byberg, F.S.Jørgensen, S.Hansen, and E.Hough (1992).
Substrate-enzyme interactions and catalytic mechanism in phospholipase C: a molecular modeling study using the GRID program.
  Proteins, 12, 331-338.  
1525782 M.Brufani, M.C.Cesta, L.Donnarumma, L.Filocamo, G.Gostoli, S.Lappa, E.Ferrari, and P.G.Pagella (1992).
Synthesis of some carbamates of myo-inositol.
  Carbohydr Res, 228, 371-376.  
1542663 T.C.Bruice, H.Y.Mei, G.X.He, and V.Lopez (1992).
Rational design of substituted tripyrrole peptides that complex with DNA by both selective minor-groove binding and electrostatic interaction with the phosphate backbone.
  Proc Natl Acad Sci U S A, 89, 1700-1704.  
  1710977 A.Volbeda, A.Lahm, F.Sakiyama, and D.Suck (1991).
Crystal structure of Penicillium citrinum P1 nuclease at 2.8 A resolution.
  EMBO J, 10, 1607-1618.  
  1779929 J.I.Rood, and S.T.Cole (1991).
Molecular genetics and pathogenesis of Clostridium perfringens.
  Microbiol Rev, 55, 621-648.  
2104979 B.L.Vallee, and D.S.Auld (1990).
Active-site zinc ligands and activated H2O of zinc enzymes.
  Proc Natl Acad Sci U S A, 87, 220-224.  
1979549 N.K.Williams, R.J.Simpson, R.L.Moritz, Y.Peide, L.Crofts, E.Minasian, S.J.Leach, R.G.Wake, and R.I.Christopherson (1990).
Location of the dihydroorotase domain within trifunctional hamster dihydroorotate synthetase.
  Gene, 94, 283-288.  
  2509427 A.Kuppe, L.M.Evans, D.A.McMillen, and O.H.Griffith (1989).
Phosphatidylinositol-specific phospholipase C of Bacillus cereus: cloning, sequencing, and relationship to other phospholipases.
  J Bacteriol, 171, 6077-6083.  
2672444 D.Eisenberg, and C.P.Hill (1989).
Protein crystallography: more surprises ahead.
  Trends Biochem Sci, 14, 260-264.  
2771946 S.R.Presnell, and F.E.Cohen (1989).
Topological distribution of four-alpha-helix bundles.
  Proc Natl Acad Sci U S A, 86, 6592-6596.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.