2c27
From Proteopedia
Line 1: | Line 1: | ||
[[Image:2c27.gif|left|200px]] | [[Image:2c27.gif|left|200px]] | ||
- | + | <!-- | |
- | + | The line below this paragraph, containing "STRUCTURE_2c27", creates the "Structure Box" on the page. | |
- | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
- | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
- | | | + | or leave the SCENE parameter empty for the default display. |
- | | | + | --> |
- | + | {{STRUCTURE_2c27| PDB=2c27 | SCENE= }} | |
- | + | ||
- | + | ||
- | }} | + | |
'''THE STRUCTURE OF MYCOTHIOL SYNTHASE IN COMPLEX WITH DES-ACETYLMYCOTHIOL AND COENZYMEA.''' | '''THE STRUCTURE OF MYCOTHIOL SYNTHASE IN COMPLEX WITH DES-ACETYLMYCOTHIOL AND COENZYMEA.''' | ||
Line 29: | Line 26: | ||
[[Category: Vetting, M W.]] | [[Category: Vetting, M W.]] | ||
[[Category: Yu, M.]] | [[Category: Yu, M.]] | ||
- | [[Category: | + | [[Category: Acetyltransferase]] |
- | [[Category: | + | [[Category: Des-acetylmycothiol]] |
- | [[Category: | + | [[Category: Gcn5 related n-acetyltransferase]] |
- | [[Category: | + | [[Category: Gnat]] |
- | [[Category: | + | [[Category: Mycobacterium tuberculosis]] |
- | [[Category: | + | [[Category: Mycothiol synthase]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 21:08:08 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 18:08, 3 May 2008
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 in the proper orientation for direct nucleophilic attack on the si-face of the acetyl group of acetyl-CoA. Glu-234 and Tyr-294 are positioned to act as a general base and general acid to promote acetyl transfer. In addition, this structure provides further evidence that the N-terminal acetyltransferase domain no longer has enzymatic activity and is vestigial in nature.
About this Structure
2C27 is a Single protein structure of sequence from Mycobacterium tuberculosis. 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 Page seeded by OCA on Sat May 3 21:08:08 2008