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Oxidoreductase PDB id
1sk7
Jmol
Contents
Protein chain
187 a.a. *
Ligands
SO4
HEM
Waters ×158
* Residue conservation analysis
PDB id:
1sk7
Name: Oxidoreductase
Title: Structural basis for novel delta-regioselective heme oxygena the opportunistic pathogen pseudomonas aeruginosa
Structure: Hypothetical protein pa-ho. Chain: a. Engineered: yes
Source: Pseudomonas aeruginosa. Organism_taxid: 287. Gene: piga. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Resolution:
1.60Å     R-factor:   0.235     R-free:   0.273
Authors: J.Friedman,L.Lad,H.Li,A.Wilks,T.L.Poulos
Key ref:
J.Friedman et al. (2004). Structural basis for novel delta-regioselective heme oxygenation in the opportunistic pathogen Pseudomonas aeruginosa. Biochemistry, 43, 5239-5245. PubMed id: 15122889 DOI: 10.1021/bi049687g
Date:
04-Mar-04     Release date:   22-Jun-04    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
O69002  (O69002_PSEAE) -  Iron-starvation protein PigA
Seq:
Struc: 		198 a.a.
187 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     oxidation-reduction process   2 terms 
  Biochemical function     heme oxygenase (decyclizing) activity     2 terms  

 

 
DOI no: 10.1021/bi049687g Biochemistry 43:5239-5245 (2004)
PubMed id: 15122889  
 
 
Structural basis for novel delta-regioselective heme oxygenation in the opportunistic pathogen Pseudomonas aeruginosa.
J.Friedman, L.Lad, H.Li, A.Wilks, T.L.Poulos.
 
  ABSTRACT  
 
The Gram-negative bacterium Pseudomonas aeruginosa contains a heme oxygenase (pa-HO) that primarily oxygenates the delta-meso heme carbon [Caignan, G. A., Deshmukh, R., Wilks, A., Zeng, Y., Huang, H. W., Moenne-Loccoz, P., Bunce, R. A., Eastman, M. A., and Rivera, M. (2002) J. Am. Chem. Soc. 124, 14879-14892]. This differs from other previously characterized heme oxygenases, which display regioselectivity for the alpha-meso heme carbon. Here we report the crystal structure of pa-HO at 1.60 A resolution and compare it to the 1.50 A structure of nm-HO from Neisseria meningitidis [Schuller, D. J., Zhu, W., Stojiljkovic, I., Wilks, A., and Poulos, T. L. (2001) Biochemistry 40, 11552-11558]. The crystal structure of pa-HO maintains the same overall fold as other bacterial and mammalian heme oxygenases, including a conserved network of hydrogen-bonded solvent molecules important for dioxygen activation. The novel delta-regioselectivity of heme oxygenation observed by pa-HO is due to the heme being rotated by approximately 100 degrees, which places the delta-meso heme carbon in the same position as the alpha-meso heme carbon in other heme oxygenases. The main interaction in pa-HO that stabilizes the unique heme orientation is a salt bridge between Lys132 and the heme 7-propionate, as well as hydrophobic contacts involving Leu29, Val33, and Phe189 with the heme methyl and vinyl groups.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
19860740 B.Gisk, Y.Yasui, T.Kohchi, and N.Frankenberg-Dinkel (2010).
Characterization of the haem oxygenase protein family in Arabidopsis thaliana reveals a diversity of functions.
  Biochem J, 425, 425-434.  
19842713 D.Peng, H.Ogura, W.Zhu, L.H.Ma, J.P.Evans, P.R.Ortiz de Montellano, and G.N.La Mar (2009).
Coupling of the distal hydrogen bond network to the exogenous ligand in substrate-bound, resting state human heme oxygenase.
  Biochemistry, 48, 11231-11242.  
19243105 H.Ogura, J.P.Evans, D.Peng, J.D.Satterlee, P.R.Ortiz de Montellano, and G.N.La Mar (2009).
The orbital ground state of the azide-substrate complex of human heme oxygenase is an indicator of distal H-bonding: implications for the enzyme mechanism.
  Biochemistry, 48, 3127-3137.  
18976815 L.H.Ma, Y.Liu, X.Zhang, T.Yoshida, and G.N.La Mar (2009).
1H NMR study of the effect of variable ligand on heme oxygenase electronic and molecular structure.
  J Inorg Biochem, 103, 10-19.  
18977196 Y.Tong, and M.Guo (2009).
Bacterial heme-transport proteins and their heme-coordination modes.
  Arch Biochem Biophys, 481, 1.  
17534527 A.Wilks, and K.A.Burkhard (2007).
Heme and virulence: how bacterial pathogens regulate, transport and utilize heme.
  Nat Prod Rep, 24, 511-522.  
17965015 C.M.Bianchetti, L.Yi, S.W.Ragsdale, and G.N.Phillips (2007).
Comparison of apo- and heme-bound crystal structures of a truncated human heme oxygenase-2.
  J Biol Chem, 282, 37624-37631.
PDB codes: 2q32 2qpp 2rgz
17095508 J.Friedman, Y.T.Meharenna, A.Wilks, and T.L.Poulos (2007).
Diatomic ligand discrimination by the heme oxygenases from Neisseria meningitidis and Pseudomonas aeruginosa.
  J Biol Chem, 282, 1066-1071.  
17534530 M.Unno, T.Matsui, and M.Ikeda-Saito (2007).
Structure and catalytic mechanism of heme oxygenase.
  Nat Prod Rep, 24, 553-570.  
17387526 Y.Tong, and M.Guo (2007).
Cloning and characterization of a novel periplasmic heme-transport protein from the human pathogen Pseudomonas aeruginosa.
  J Biol Inorg Chem, 12, 735-750.  
16698925 G.O.Paiva-Silva, C.Cruz-Oliveira, E.S.Nakayasu, C.M.Maya-Monteiro, B.C.Dunkov, H.Masuda, I.C.Almeida, and P.L.Oliveira (2006).
A heme-degradation pathway in a blood-sucking insect.
  Proc Natl Acad Sci U S A, 103, 8030-8035.  
16388581 J.Wang, J.P.Evans, H.Ogura, G.N.La Mar, and P.R.Ortiz de Montellano (2006).
Alteration of the regiospecificity of human heme oxygenase-1 by unseating of the heme but not disruption of the distal hydrogen bonding network.
  Biochemistry, 45, 61-73.  
16704267 L.H.Ma, Y.Liu, X.Zhang, T.Yoshida, and G.N.La Mar (2006).
1H NMR study of the magnetic properties and electronic structure of the hydroxide complex of substrate-bound heme oxygenase from Neisseria meningitidis: influence of the axial water deprotonation on the distal H-bond network.
  J Am Chem Soc, 128, 6657-6668.  
16683803 L.H.Ma, Y.Liu, X.Zhang, T.Yoshida, K.C.Langry, K.M.Smith, and G.N.La Mar (2006).
Modulation of the axial water hydrogen-bonding properties by chemical modification of the substrate in resting state, substrate-bound heme oxygenase from Neisseria meningitidis; coupling to the distal H-bond network via ordered water molecules.
  J Am Chem Soc, 128, 6391-6399.  
17023414 M.D.Suits, N.Jaffer, and Z.Jia (2006).
Structure of the Escherichia coli O157:H7 heme oxygenase ChuS in complex with heme and enzymatic inactivation by mutation of the heme coordinating residue His-193.
  J Biol Chem, 281, 36776-36782.
PDB code: 2hq2
16981723 M.N.Bhakta, and A.Wilks (2006).
The mechanism of heme transfer from the cytoplasmic heme binding protein PhuS to the delta-regioselective heme oxygenase of Pseudomonas aeruginosa.
  Biochemistry, 45, 11642-11649.  
16548515 Y.Liu, L.H.Ma, X.Zhang, T.Yoshida, J.D.Satterlee, and G.N.La Mar (2006).
Characterization of the spontaneous "aging" of the heme oxygenase from the pathological bacterium Neisseria meningitidis via cleavage of the C-terminus in contact with the substrate. Implications for functional studies and the crystal structure.
  Biochemistry, 45, 3875-3886.  
15525643 J.Wang, L.Lad, T.L.Poulos, and P.R.Ortiz de Montellano (2005).
Regiospecificity determinants of human heme oxygenase: differential NADPH- and ascorbate-dependent heme cleavage by the R183E mutant.
  J Biol Chem, 280, 2797-2806.
PDB codes: 1xk2 1xk3
15735347 L.Lehtiö, I.Fabrichniy, T.Hansen, P.Schönheit, and A.Goldman (2005).
Unusual twinning in an acetyl coenzyme A synthetase (ADP-forming) from Pyrococcus furiosus.
  Acta Crystallogr D Biol Crystallogr, 61, 350-354.  
16275907 M.D.Suits, G.P.Pal, K.Nakatsu, A.Matte, M.Cygler, and Z.Jia (2005).
Identification of an Escherichia coli O157:H7 heme oxygenase with tandem functional repeats.
  Proc Natl Acad Sci U S A, 102, 16955-16960.
PDB code: 1u9t
15528205 T.Matsui, M.Furukawa, M.Unno, T.Tomita, and M.Ikeda-Saito (2005).
Roles of distal Asp in heme oxygenase from Corynebacterium diphtheriae, HmuO: A water-driven oxygen activation mechanism.
  J Biol Chem, 280, 2981-2989.
PDB codes: 1wnv 1wnw 1wnx
15297453 J.Wang, F.Niemevz, L.Lad, L.Huang, D.E.Alvarez, G.Buldain, T.L.Poulos, and P.R.de Montellano (2004).
Human heme oxygenase oxidation of 5- and 15-phenylhemes.
  J Biol Chem, 279, 42593-42604.
PDB codes: 1s13 1t5p
15310749 R.Wegele, R.Tasler, Y.Zeng, M.Rivera, and N.Frankenberg-Dinkel (2004).
The heme oxygenase(s)-phytochrome system of Pseudomonas aeruginosa.
  J Biol Chem, 279, 45791-45802.  
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.