2bzr

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{{STRUCTURE_2bzr| PDB=2bzr | SCENE= }}
{{STRUCTURE_2bzr| PDB=2bzr | SCENE= }}
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'''CRYSTAL STRUCTURE OF ACCD5 (RV3280), AN ACYL-COA CARBOXYLASE BETA-SUBUNIT FROM MYCOBACTERIUM TUBERCULOSIS'''
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===CRYSTAL STRUCTURE OF ACCD5 (RV3280), AN ACYL-COA CARBOXYLASE BETA-SUBUNIT FROM MYCOBACTERIUM TUBERCULOSIS===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 17157300 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17157300}}
==About this Structure==
==About this Structure==
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[[Category: Transferase]]
[[Category: Transferase]]
[[Category: Xmtb]]
[[Category: Xmtb]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 21:01:40 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 09:18:43 2008''

Revision as of 06:18, 29 July 2008

Image:2bzr.png

Template:STRUCTURE 2bzr

CRYSTAL STRUCTURE OF ACCD5 (RV3280), AN ACYL-COA CARBOXYLASE BETA-SUBUNIT FROM MYCOBACTERIUM TUBERCULOSIS

Template:ABSTRACT PUBMED 17157300

About this Structure

2BZR is a Single protein structure of sequence from Mycobacterium tuberculosis. 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

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