1ozp: Difference between revisions

Revision as of 07:48, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1ozp.png

Template:STRUCTURE 1ozp

Crystal Structure of Rv0819 from Mycobacterium tuberculosis MshD-Mycothiol Synthase Acetyl-Coenzyme A Complex.Crystal Structure of Rv0819 from Mycobacterium tuberculosis MshD-Mycothiol Synthase Acetyl-Coenzyme A Complex.

Template:ABSTRACT PUBMED 12930994

About this StructureAbout this Structure

1OZP is a Single protein structure of sequence from Mycobacterium tuberculosis h37rv. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of mycothiol synthase (Rv0819) from Mycobacterium tuberculosis shows structural homology to the GNAT family of N-acetyltransferases., Vetting MW, Roderick SL, Yu M, Blanchard JS, Protein Sci. 2003 Sep;12(9):1954-9. PMID:12930994

Page seeded by OCA on Mon Jul 28 07:48:03 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:1ozp.jpg|left|200px]]
+{{Seed}}
+[[Image:1ozp.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1ozp|  PDB=1ozp  |  SCENE=  }}
-'''Crystal Structure of Rv0819 from Mycobacterium tuberculosis MshD-Mycothiol Synthase Acetyl-Coenzyme A Complex.'''
+===Crystal Structure of Rv0819 from Mycobacterium tuberculosis MshD-Mycothiol Synthase Acetyl-Coenzyme A Complex.===
-==Overview==
+<!--
-Mycothiol is the predominant low-molecular weight thiol produced by actinomycetes, including Mycobacterium tuberculosis. The last reaction in the biosynthetic pathway for mycothiol is catalyzed by mycothiol synthase (MshD), which acetylates the cysteinyl amine of cysteine-glucosamine-inositol (Cys-GlcN-Ins). The crystal structure of MshD was determined in the presence of coenzyme A and acetyl-CoA. MshD consists of two tandem-repeated domains, each exhibiting the Gcn5-related N-acetyltransferase (GNAT) fold. These two domains superimpose with a root-mean-square deviation of 1.7 A over 88 residues, and each was found to bind one molecule of coenzyme, although the binding sites are quite different. The C-terminal domain has a similar active site to many GNAT members in which the acetyl group of the coenzyme is presented to an open active site slot. However, acetyl-CoA bound to the N-terminal domain is buried, and is apparently not positioned to promote acetyl transfer. A modeled substrate complex indicates that Cys-GlcN-Ins would only fill a portion of a negatively charged channel located between the two domains. This is the first structure determined for an enzyme involved in the biosynthesis of mycothiol.
+The line below this paragraph, {{ABSTRACT_PUBMED_12930994}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12930994 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12930994}}
 ==About this Structure==
@@ Line 30: / Line 34: @@
 [[Category: Gnat fold]]
 [[Category: Mshd]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 04:29:13 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 07:48:03 2008''