1i1d
From Proteopedia
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| - | [[Image:1i1d.gif|left|200px]] | + | [[Image:1i1d.gif|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF YEAST GNA1 BOUND TO COA AND GLNAC-6P''' | + | {{Structure |
| + | |PDB= 1i1d |SIZE=350|CAPTION= <scene name='initialview01'>1i1d</scene>, resolution 1.80Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=16G:N-ACETYL-D-GLUCOSAMINE-6-PHOSPHATE'>16G</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene> and <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Glucosamine_6-phosphate_N-acetyltransferase Glucosamine 6-phosphate N-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.4 2.3.1.4] | ||
| + | |GENE= YFL017C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF YEAST GNA1 BOUND TO COA AND GLNAC-6P''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1I1D is a [ | + | 1I1D is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I1D OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11278591 11278591] |
[[Category: Glucosamine 6-phosphate N-acetyltransferase]] | [[Category: Glucosamine 6-phosphate N-acetyltransferase]] | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
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[[Category: gnat conserved core]] | [[Category: gnat conserved core]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:44:15 2008'' |
Revision as of 09:44, 20 March 2008
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| , resolution 1.80Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , and | ||||||
| Gene: | YFL017C (Saccharomyces cerevisiae) | ||||||
| Activity: | Glucosamine 6-phosphate N-acetyltransferase, with EC number 2.3.1.4 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF YEAST GNA1 BOUND TO COA AND GLNAC-6P
Overview
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.
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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