Structural diversity in the six-fold redundant set of acyl-CoA carboxyltransferases in Mycobacterium tuberculosis.

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.

• Authors: Simon J Holton, Stephanie King-Scott, Ali Nasser Eddine, Stefan H E Kaufmann, Matthias Wilmanns
• Journal: FEBS letters (FEBS Lett) Vol. 580 Issue 30 Pg. 6898-902 (Dec 22 2006) ISSN: 0014-5793 [Print] England
• PMID: 17157300 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Acyl Coenzyme A
• Protein Subunits
• Carboxyl and Carbamoyl Transferases

Topics

• Acyl Coenzyme A (metabolism)
• Binding Sites
• Carboxyl and Carbamoyl Transferases (chemistry, genetics, metabolism)
• Crystallography, X-Ray
• Models, Molecular
• Mycobacterium tuberculosis (enzymology, genetics)
• Protein Binding
• Protein Folding
• Protein Structure, Quaternary
• Protein Subunits (genetics, metabolism)