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PDBsum entry 3e4y

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protein ligands links
Oxidoreductase PDB id
3e4y
Jmol
Contents
Protein chain
301 a.a. *
Ligands
HEM
GOL ×2
PO4
Waters ×122
* Residue conservation analysis
PDB id:
3e4y
Name: Oxidoreductase
Title: Crystal structure of a 33kda catalase-related protein from mycobacterium avium subsp. Paratuberculosis. I2(1)2(1)2(1) form
Structure: Putative uncharacterized protein. Chain: a. Engineered: yes
Source: Mycobacterium avium subsp. Paratubercu organism_taxid: 1770. Gene: map_2744c. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.60Å     R-factor:   0.202     R-free:   0.257
Authors: S.Pakhomova,M.E.Newcomer
Key ref: S.Pakhomova et al. (2009). The structure and peroxidase activity of a 33-kDa catalase-related protein from Mycobacterium avium ssp. paratuberculosis. Protein Sci, 18, 2559-2568. PubMed id: 19827095
Date:
12-Aug-08     Release date:   18-Aug-09    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q73WB6  (Q73WB6_MYCPA) -  Catalase-related peroxidase
Seq:
Struc:
313 a.a.
301 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     regulation of reactive oxygen species metabolic process   4 terms 
  Biochemical function     oxidoreductase activity     6 terms  

 

 
Protein Sci 18:2559-2568 (2009)
PubMed id: 19827095  
 
 
The structure and peroxidase activity of a 33-kDa catalase-related protein from Mycobacterium avium ssp. paratuberculosis.
S.Pakhomova, B.Gao, W.E.Boeglin, A.R.Brash, M.E.Newcomer.
 
  ABSTRACT  
 
True catalases are tyrosine-liganded, usually tetrameric, hemoproteins with subunit sizes of approximately 55-84 kDa. Recently characterized hemoproteins with a catalase-related structure, yet lacking in catalatic activity, include the 40-43 kDa allene oxide synthases of marine invertebrates and cyanobacteria. Herein, we describe the 1.8 A X-ray crystal structure of a 33 kDa subunit hemoprotein from Mycobacterium avium ssp. paratuberculosis (annotated as MAP-2744c), that retains the core elements of the catalase fold and exhibits an organic peroxide-dependent peroxidase activity. MAP-2744c exhibits negligible catalatic activity, weak peroxidatic activity using hydrogen peroxide (20/s) and strong peroxidase activity (approximately 300/s) using organic hydroperoxides as co-substrate. Key amino acid differences significantly impact prosthetic group conformation and placement and confer a distinct activity to this prototypical member of a group of conserved bacterial "minicatalases". Its structural features and the result of the enzyme assays support a role for MAP-2744c and its close homologues in mitigating challenge by a variety of reactive oxygen species.