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PDBsum entry 1qqw

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protein ligands Protein-protein interface(s) links
Oxidoreductase PDB id
1qqw
Jmol
Contents
Protein chain
499 a.a. *
Ligands
HEM ×4
Waters ×393
* Residue conservation analysis
PDB id:
1qqw
Name: Oxidoreductase
Title: Crystal structure of human erythrocyte catalase
Structure: Catalase. Chain: a, b, c, d. Ec: 1.11.1.6
Source: Homo sapiens. Human. Organism_taxid: 9606. Tissue: blood. Cell: erythrocyte
Biol. unit: Tetramer (from PQS)
Resolution:
2.75Å     R-factor:   0.206     R-free:   0.272
Authors: T.P.Ko,M.K.Safo,F.N.Musayev,C.Wang,S.H.Wu,D.J.Abraham
Key ref:
T.P.Ko et al. (2000). Structure of human erythrocyte catalase. Acta Crystallogr D Biol Crystallogr, 56, 241-245. PubMed id: 10666617 DOI: 10.1107/S0907444999015930
Date:
09-Jun-99     Release date:   14-Jun-99    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P04040  (CATA_HUMAN) -  Catalase
Seq:
Struc:
 
Seq:
Struc:
527 a.a.
499 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.1.11.1.6  - 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+)
Heme
Bound ligand (Het Group name = HEM) matches with 95.00% similarity
Mn(2+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     membrane   13 terms 
  Biological process     small molecule metabolic process   29 terms 
  Biochemical function     antioxidant activity     12 terms  

 

 
    reference    
 
 
DOI no: 10.1107/S0907444999015930 Acta Crystallogr D Biol Crystallogr 56:241-245 (2000)
PubMed id: 10666617  
 
 
Structure of human erythrocyte catalase.
T.P.Ko, M.K.Safo, F.N.Musayev, M.L.Di Salvo, C.Wang, S.H.Wu, D.J.Abraham.
 
  ABSTRACT  
 
Catalase (E.C. 1.11.1.6) was purified from human erythrocytes and crystallized in three different forms: orthorhombic, hexagonal and tetragonal. The structure of the orthorhombic crystal form of human erythrocyte catalase (HEC), with space group P2(1)2(1)2(1) and unit-cell parameters a = 84.9, b = 141.7, c = 232.5 A, was determined and refined with 2.75 A resolution data. Non-crystallographic symmetry restraints were employed and the resulting R value and R(free) were 0.206 and 0.272, respectively. The overall structure and arrangement of HEC molecules in the orthorhombic unit cell were very similar to those of bovine liver catalase (BLC). However, no NADPH was observed in the HEC crystal and a water was bound to the active-site residue His75. Conserved lattice interactions suggested a common growth mechanism for the orthorhombic crystals of HEC and BLC.
 
  Selected figure(s)  
 
Figure 2.
Figure 2 Superposition of the HEC (colored blue) and BLC (colored purple) models. The C^ atoms of the variable residues are shown in green. Heme groups are shown in red. The NADPH molecules which were observed in BLC but not in HEC are shown in yellow. The figure was drawn using GRASP.
 
  The above figure is reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2000, 56, 241-245) copyright 2000.  
  Figure was selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20056148 M.Rusu, and S.Birmanns (2010).
Evolutionary tabu search strategies for the simultaneous registration of multiple atomic structures in cryo-EM reconstructions.
  J Struct Biol, 170, 164-171.  
19827095 S.Pakhomova, B.Gao, W.E.Boeglin, A.R.Brash, and M.E.Newcomer (2009).
The structure and peroxidase activity of a 33-kDa catalase-related protein from Mycobacterium avium ssp. paratuberculosis.
  Protein Sci, 18, 2559-2568.
PDB codes: 3e4w 3e4y
18652800 B.Gao, W.E.Boeglin, and A.R.Brash (2008).
Role of the conserved distal heme asparagine of coral allene oxide synthase (Asn137) and human catalase (Asn148): mutations affect the rate but not the essential chemistry of the enzymatic transformations.
  Arch Biochem Biophys, 477, 285-290.  
18722522 Z.He, S.Yu, G.Mei, M.Zheng, M.Wang, Y.Dai, B.Tang, and N.Li (2008).
Maternally transmitted milk containing recombinant human catalase provides protection against oxidation for mouse offspring during lactation.
  Free Radic Biol Med, 45, 1135-1142.  
17822396 J.I.Koepke, K.A.Nakrieko, C.S.Wood, K.K.Boucher, L.J.Terlecky, P.A.Walton, and S.R.Terlecky (2007).
Restoration of peroxisomal catalase import in a model of human cellular aging.
  Traffic, 8, 1590-1600.  
17552919 M.Niepmann (2007).
Discontinuous native protein gel electrophoresis: pros and cons.
  Expert Rev Proteomics, 4, 355-361.  
12730222 D.E.Heck, A.M.Vetrano, T.M.Mariano, and J.D.Laskin (2003).
UVB light stimulates production of reactive oxygen species: unexpected role for catalase.
  J Biol Chem, 278, 22432-22436.  
11455600 W.Melik-Adamyan, J.Bravo, X.Carpena, J.Switala, M.J.Maté, I.Fita, and P.C.Loewen (2001).
Substrate flow in catalases deduced from the crystal structures of active site variants of HPII from Escherichia coli.
  Proteins, 44, 270-281.
PDB codes: 1gg9 1gge 1ggf 1ggh 1ggj 1ggk
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.