1p0h

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[[Image:1p0h.jpg|left|200px]]
[[Image:1p0h.jpg|left|200px]]
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{{Structure
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|PDB= 1p0h |SIZE=350|CAPTION= <scene name='initialview01'>1p0h</scene>, resolution 1.60&Aring;
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The line below this paragraph, containing "STRUCTURE_1p0h", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY=
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|GENE= Rv0819 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83332 Mycobacterium tuberculosis H37Rv])
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|DOMAIN=
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{{STRUCTURE_1p0h| PDB=1p0h | SCENE= }}
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|RELATEDENTRY=[[1ozp|1OZP]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1p0h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p0h OCA], [http://www.ebi.ac.uk/pdbsum/1p0h PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1p0h RCSB]</span>
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}}
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'''Crystal Structure of Rv0819 from Mycobacterium Tuberculosis MshD-Mycothiol Synthase Coenzyme A Complex'''
'''Crystal Structure of Rv0819 from Mycobacterium Tuberculosis MshD-Mycothiol Synthase Coenzyme A Complex'''
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[[Category: Vetting, M W.]]
[[Category: Vetting, M W.]]
[[Category: Yu, M.]]
[[Category: Yu, M.]]
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[[Category: acetyltransferase]]
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[[Category: Acetyltransferase]]
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[[Category: coenzyme a complex]]
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[[Category: Coenzyme a complex]]
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[[Category: gnat fold]]
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[[Category: Gnat fold]]
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[[Category: mshd]]
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[[Category: Mshd]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:31:33 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:52:59 2008''
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Revision as of 01:31, 3 May 2008

Template:STRUCTURE 1p0h

Crystal Structure of Rv0819 from Mycobacterium Tuberculosis MshD-Mycothiol Synthase 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.

About this Structure

1P0H is a Single protein structure of sequence from Mycobacterium tuberculosis h37rv. Full crystallographic information is available from OCA.

Reference

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 Sat May 3 04:31:33 2008

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