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PDBsum entry 2bzr

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protein Protein-protein interface(s) links
Transferase PDB id
2bzr
Jmol
Contents
Protein chains
(+ 0 more) 512 a.a. *
Waters ×1690
* Residue conservation analysis
PDB id:
2bzr
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
Resolution:
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
Date:
22-Aug-05     Release date:   02-Jan-07    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam  
P9WQH7  (PCC5_MYCTU) -  Probable propionyl-CoA carboxylase beta chain 5
Seq:
Struc:
 
Seq:
Struc:
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.6.4.1.3  - Propionyl-CoA carboxylase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + propanoyl-CoA + HCO3- = ADP + phosphate + (S)-methylmalonyl- CoA
ATP
+ propanoyl-CoA
+ HCO(3)(-)
= ADP
+ phosphate
+ (S)-methylmalonyl- CoA
      Cofactor: Biotin
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  

 

 
    reference    
 
 
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.
 
  ABSTRACT  
 
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.  
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.