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2c27
From Proteopedia
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[[Category: mycothiol synthase]] | [[Category: mycothiol synthase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 10:48:01 2007'' |
Revision as of 08:43, 30 October 2007
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THE STRUCTURE OF MYCOTHIOL SYNTHASE IN COMPLEX WITH DES-ACETYLMYCOTHIOL AND COENZYMEA.
Overview
The structure of the ternary complex of mycothiol synthase from, Mycobacterium tuberculosis with bound desacetylmycothiol and CoA was, determined to 1.8 A resolution. The structure of the acetyl-CoA-binary, complex had shown an active site groove that was several times larger than, its substrate. The structure of the ternary complex reveals that mycothiol, synthase undergoes a large conformational change in which the two, acetyltransferase domains are brought together through shared interactions, with the functional groups of desacetylmycothiol, thereby decreasing the, size of this large central groove. A comparison of the binary and ternary, structures illustrates many of the features that promote catalysis., Desacetylmycothiol is positioned with its primary amine in close proximity, and ... [(full description)]
About this Structure
2C27 is a [Single protein] structure of sequence from [Mycobacterium tuberculosis] with ACO, COA and MA8 as [ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
The substrate-induced conformational change of Mycobacterium tuberculosis mycothiol synthase., Vetting MW, Yu M, Rendle PM, Blanchard JS, J Biol Chem. 2006 Feb 3;281(5):2795-802. Epub 2005 Dec 2. PMID:16326705
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