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2bzr
From Proteopedia
| 2bzr, resolution 2.20Å () | |||||||||
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| Activity: | Propionyl-CoA carboxylase, with EC number 6.4.1.3 | ||||||||
| Domains: | PRK05724, AccD, COG4799 | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB, TOPSAN | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
CRYSTAL STRUCTURE OF ACCD5 (RV3280), AN ACYL-COA CARBOXYLASE BETA-SUBUNIT FROM MYCOBACTERIUM TUBERCULOSIS
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.
Structural diversity in the six-fold redundant set of acyl-CoA carboxyltransferases in Mycobacterium tuberculosis., Holton SJ, King-Scott S, Nasser Eddine A, Kaufmann SH, Wilmanns M, FEBS Lett. 2006 Dec 22;580(30):6898-902. Epub 2006 Nov 30. PMID:17157300
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
2BZR is a 6 chains structure of sequences from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.
Reference
- Holton SJ, King-Scott S, Nasser Eddine A, Kaufmann SH, Wilmanns M. Structural diversity in the six-fold redundant set of acyl-CoA carboxyltransferases in Mycobacterium tuberculosis. FEBS Lett. 2006 Dec 22;580(30):6898-902. Epub 2006 Nov 30. PMID:17157300
Page seeded by OCA on Wed Feb 18 02:41:51 2009
