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PDBsum entry 4g7a

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protein ligands metals Protein-protein interface(s) links
Lyase PDB id
4g7a
Jmol
Contents
Protein chains
224 a.a.
Ligands
AZM ×2
Metals
_ZN ×2
Waters ×564
PDB id:
4g7a
Name: Lyase
Title: The crystal structure of an alpha carbonic anhydrase from th extremophilic bacterium sulfurihydrogenibium yellowstonense
Structure: Carbonate dehydratase. Chain: a, b. Fragment: unp residues 21-246. Synonym: alpha-carbonic anhydrase. Engineered: yes
Source: Sulfurihydrogenibium sp. Yo3aop1. Sulfurihydrogenibium yellowstonense. Organism_taxid: 436114. Gene: syo3aop1_0578. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
1.80Å     R-factor:   0.168     R-free:   0.203
Authors: A.Di Fiore,G.De Simone
Key ref: A.Di Fiore et al. (2013). X-ray structure of the first `extremo-α-carbonic anhydrase', a dimeric enzyme from the thermophilic bacterium Sulfurihydrogenibium yellowstonense YO3AOP1. Acta Crystallogr D Biol Crystallogr, 69, 1150-1159. PubMed id: 23695259 DOI: 10.1107/S0907444913007208
Date:
20-Jul-12     Release date:   29-May-13    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
B2V8E3  (B2V8E3_SULSY) -  Carbonate dehydratase
Seq:
Struc:
246 a.a.
224 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.4.2.1.1  - Carbonate dehydratase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: H2CO3 = CO2 + H2O
H(2)CO(3)
= CO(2)
+ H(2)O
      Cofactor: Zn(2+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     one-carbon metabolic process   1 term 
  Biochemical function     carbonate dehydratase activity     2 terms  

 

 
    Added reference    
 
 
DOI no: 10.1107/S0907444913007208 Acta Crystallogr D Biol Crystallogr 69:1150-1159 (2013)
PubMed id: 23695259  
 
 
X-ray structure of the first `extremo-α-carbonic anhydrase', a dimeric enzyme from the thermophilic bacterium Sulfurihydrogenibium yellowstonense YO3AOP1.
A.Di Fiore, C.Capasso, V.De Luca, S.M.Monti, V.Carginale, C.T.Supuran, A.Scozzafava, C.Pedone, M.Rossi, G.De Simone.
 
  ABSTRACT  
 
SspCA, a novel `extremo-α-carbonic anhydrase' isolated from the thermophilic bacterium Sulfurihydrogenibium yellowstonense YO3AOP1, is an efficient catalyst for the hydration of CO2 and presents exceptional thermostability. Indeed, SspCA retains a high catalytic activity even after being heated to 343-373 K for several hours. Here, the crystallographic structure of this α-carbonic anhydrase (α-CA) is reported and the factors responsible for its function at high temperature are elucidated. In particular, the study suggests that increased structural compactness, together with an increased number of charged residues on the protein surface and a greater number of ionic networks, seem to be the key factors involved in the higher thermostability of this enzyme with respect to its mesophilic homologues. These findings are of extreme importance, since they provide a structural basis for the understanding of the mechanisms responsible for thermal stability in the α-CA family for the first time. The data obtained offer a tool that can be exploited to engineer α-CAs in order to obtain enzymes with enhanced thermostability for use in the harsh conditions of the CO2 capture and sequestration processes.