2bzr
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(New page: 200px<br /><applet load="2bzr" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bzr, resolution 2.200Å" /> '''CRYSTAL STRUCTURE O...)
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Revision as of 06:50, 21 November 2007
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CRYSTAL STRUCTURE OF ACCD5 (RV3280), AN ACYL-COA CARBOXYLASE BETA-SUBUNIT FROM MYCOBACTERIUM TUBERCULOSIS
Overview
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.
About this Structure
2BZR is a Single protein structure of sequence from Mycobacterium tuberculosis. Active as Propionyl-CoA carboxylase, with EC number 6.4.1.3 Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Wed Nov 21 08:58:06 2007
Categories: Mycobacterium tuberculosis | Propionyl-CoA carboxylase | Single protein | Holton, S.J. | XMTB, Mycobacterium.Tuberculosis.Structural.Proteomics.Project. | Accase | Fatty acid biosynthesis | Ligase | Mycobacterium tuberculosis structural proteomics project | Structural genomics | Transferase | Xmtb