PDBsum entry 1ye9

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protein ligands Protein-protein interface(s) links
Oxidoreductase PDB id
Protein chains
(+ 2 more) 223 a.a. *
(+ 2 more) 256 a.a. *
HDD ×8
Waters ×180
* Residue conservation analysis
PDB id:
Name: Oxidoreductase
Title: Crystal structure of proteolytically truncated catalase hpii from e. Coli
Structure: Catalase hpii. Chain: a, b, c, d, i, j, k, l. Fragment: proteolytic fragment, residues 75-300. Engineered: yes. Catalase hpii. Chain: e, f, g, h, m, n, o, p. Fragment: proteolytic fragment, residues 309-567. Engineered: yes
Source: Escherichia coli. Organism_taxid: 562. Strain: mp180. Gene: kate. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Octamer (from PQS)
2.80Å     R-factor:   0.220     R-free:   0.269
Authors: P.C.Loewen,P.Chelikani,X.Carpena,I.Fita,R.Perez-Luque, L.J.Donald,J.Switala,H.W.Duckworth
Key ref:
P.Chelikani et al. (2005). Characterization of a large subunit catalase truncated by proteolytic cleavage. Biochemistry, 44, 5597-5605. PubMed id: 15823018 DOI: 10.1021/bi047277m
28-Dec-04     Release date:   26-Apr-05    
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Protein chains
Pfam   ArchSchema ?
P21179  (CATE_ECOLI) -  Catalase HPII
753 a.a.
223 a.a.
Protein chains
Pfam   ArchSchema ?
P21179  (CATE_ECOLI) -  Catalase HPII
753 a.a.
256 a.a.
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: Chains A, E, B, F, C, G, D, H, I, M, J, N, K, O, L, P: E.C.  - Catalase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: 2 H2O2 = O2 + 2 H2O
2 × H(2)O(2)
= O(2)
+ 2 × H(2)O
      Cofactor: Heme; Mn(2+)
Bound ligand (Het Group name = HDD) matches with 93.00% similarity
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     oxidation-reduction process   2 terms 
  Biochemical function     catalase activity     2 terms  


DOI no: 10.1021/bi047277m Biochemistry 44:5597-5605 (2005)
PubMed id: 15823018  
Characterization of a large subunit catalase truncated by proteolytic cleavage.
P.Chelikani, X.Carpena, R.Perez-Luque, L.J.Donald, H.W.Duckworth, J.Switala, I.Fita, P.C.Loewen.
The large subunit catalase HPII from Escherichia coli can be truncated by proteolysis to a structure similar to small subunit catalases. Mass spectrometry analysis indicates that there is some heterogeneity in the precise cleavage sites, but approximately 74 N-terminal residues, 189 C-terminal residues, and a 9-11-residue internal fragment, including residues 298-308, are removed. Crystal structure refinement at 2.8 A reveals that the tertiary and quaternary structure of the native enzyme is retained with only very subtle changes despite the loss of 36% of the sequence. The truncated variant exhibits a 1.8 times faster turnover rate and enhanced sensitivity to high concentrations of H(2)O(2), consistent with easier access of the substrate to the active site. In addition, the truncated variant is more sensitive to inhibition, particularly by reagents such as aminotriazole and azide which are larger than substrate H(2)O(2). The main channel leading to the heme cavity is largely unaffected by the truncation, but the lateral channel is shortened and its entrance widened by removal of the C-terminal domain, providing an explanation for easier access to the active site. Opening of the entrance to the lateral channel also opens the putative NADPH binding site, but NADPH binding could not be demonstrated. Despite the lack of bound NADPH, the compound I species of both native and truncated HPII are reduced back to the resting state with compound II being evident in the absorbance spectrum only of the heme b-containing H392A variant.