PDBsum entry 2bzr

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protein Protein-protein interface(s) links
Transferase PDB id
Protein chains
(+ 0 more) 512 a.a. *
Waters ×1690
* Residue conservation analysis
PDB id:
Name: Transferase
Title: Crystal structure of accd5 (rv3280), an acyl-coa carboxylase beta-subunit from mycobacterium tuberculosis
Structure: Propionyl-coa carboxylase beta chain 5. Chain: a, b, c, d, e, f. Synonym: acyl-coa carboxytransferase, pccase, propanoyl-coa carbon dioxide ligase. Engineered: yes
Source: Mycobacterium tuberculosis. Organism_taxid: 83332. Strain: h37rv. Expressed in: escherichia coli. Expression_system_taxid: 562
2.20Å     R-factor:   0.178     R-free:   0.211
Authors: S.J.Holton
Key ref: S.J.Holton et al. (2006). Structural diversity in the six-fold redundant set of acyl-CoA carboxyltransferases in Mycobacterium tuberculosis. FEBS Lett, 580, 6898-6902. PubMed id: 17157300 DOI: 10.1016/j.febslet.2006.11.054
22-Aug-05     Release date:   02-Jan-07    
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Protein chains
P9WQH7  (PCC5_MYCTU) -  Probable propionyl-CoA carboxylase beta chain 5
548 a.a.
512 a.a.*
Key:    Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.  - Propionyl-CoA carboxylase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + propanoyl-CoA + HCO3- = ADP + phosphate + (S)-methylmalonyl- CoA
+ propanoyl-CoA
+ HCO(3)(-)
+ phosphate
+ (S)-methylmalonyl- CoA
      Cofactor: Biotin
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     metabolic process   1 term 
  Biochemical function     nucleotide binding     4 terms  


DOI no: 10.1016/j.febslet.2006.11.054 FEBS Lett 580:6898-6902 (2006)
PubMed id: 17157300  
Structural diversity in the six-fold redundant set of acyl-CoA carboxyltransferases in Mycobacterium tuberculosis.
S.J.Holton, S.King-Scott, A.Nasser Eddine, S.H.Kaufmann, M.Wilmanns.
Mycobacterium tuberculosis contains multiple versions of the accA and accD genes that encode the alpha- and beta-subunits of at least three distinct multi-functional acyl-CoA carboxylase complexes. Because of its proposed involvement in pathogenic M. tuberculosis survival, the high-resolution crystal structure of the beta-subunit gene accD5 product has been determined and reveals a hexameric 356 kDa complex. Analysis of the active site properties of AccD5 and homology models of the other five M. tuberculosis AccD homologues reveals unexpected differences in their surface composition, providing a molecular rational key for a sorting mechanism governing correct acyl-CoA carboxylase holo complex assembly in M. tuberculosis.

Literature references that cite this PDB file's key reference

  PubMed id Reference
17483212 R.Gande, L.G.Dover, K.Krumbach, G.S.Besra, H.Sahm, T.Oikawa, and L.Eggeling (2007).
The two carboxylases of Corynebacterium glutamicum essential for fatty acid and mycolic acid synthesis.
  J Bacteriol, 189, 5257-5264.  
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