1i1d

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{{STRUCTURE_1i1d| PDB=1i1d | SCENE= }}
{{STRUCTURE_1i1d| PDB=1i1d | SCENE= }}
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'''CRYSTAL STRUCTURE OF YEAST GNA1 BOUND TO COA AND GLNAC-6P'''
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===CRYSTAL STRUCTURE OF YEAST GNA1 BOUND TO COA AND GLNAC-6P===
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==Overview==
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The yeast enzymes involved in UDP-GlcNAc biosynthesis are potential targets for antifungal agents. GNA1, a novel member of the Gcn5-related N-acetyltransferase (GNAT) superfamily, participates in UDP-GlcNAc biosynthesis by catalyzing the formation of GlcNAc6P from AcCoA and GlcN6P. We have solved three crystal structures corresponding to the apo Saccharomyces cerevisiae GNA1, the GNA1-AcCoA, and the GNA1-CoA-GlcNAc6P complexes and have refined them to 2.4, 1.3, and 1.8 A resolution, respectively. These structures not only reveal a stable, beta-intertwined, dimeric assembly with the GlcNAc6P binding site located at the dimer interface but also shed light on the catalytic machinery of GNA1 at an atomic level. Hence, they broaden our understanding of structural features required for GNAT activity, provide structural details for related aminoglycoside N-acetyltransferases, and highlight the adaptability of the GNAT superfamily members to acquire various specificities.
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(as it appears on PubMed at http://www.pubmed.gov), where 11278591 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11278591}}
==About this Structure==
==About this Structure==
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[[Category: Domain swapping]]
[[Category: Domain swapping]]
[[Category: Gnat conserved core]]
[[Category: Gnat conserved core]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:27:38 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 10:16:02 2008''

Revision as of 07:16, 1 July 2008

Image:1i1d.png

Template:STRUCTURE 1i1d

CRYSTAL STRUCTURE OF YEAST GNA1 BOUND TO COA AND GLNAC-6P

Template:ABSTRACT PUBMED 11278591

About this Structure

1I1D is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

The crystal structures of Apo and complexed Saccharomyces cerevisiae GNA1 shed light on the catalytic mechanism of an amino-sugar N-acetyltransferase., Peneff C, Mengin-Lecreulx D, Bourne Y, J Biol Chem. 2001 May 11;276(19):16328-34. Epub 2001 Feb 9. PMID:11278591

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