2c27

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Revision as of 17:45, 29 October 2007 by OCA (talk | contribs) (New page: left|200px<br /> <applet load="2c27" size="450" color="white" frame="true" align="right" spinBox="true" caption="2c27, resolution 1.80Å" /> '''THE STRUCTURE OF MY...)
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File:2c27.gif


2c27, resolution 1.80Å

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THE STRUCTURE OF MYCOTHIOL SYNTHASE IN COMPLEX WITH DES-ACETYLMYCOTHIOL AND COENZYMEA.

OverviewOverview

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 StructureAbout this Structure

2C27 is a [Single protein] structure of sequence from [Mycobacterium tuberculosis] with ACO, COA and MA8 as [ligands]. Full crystallographic information is available from [OCA].

ReferenceReference

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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