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

File:2c27.gif


2c27, resolution 1.80Å

Drag the structure with the mouse to rotate

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]. Structure known Active Site: AC1. 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

Page seeded by OCA on Tue Oct 30 16:55:24 2007

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA