1i12: Difference between revisions
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[[Image:1i12.jpg|left|200px]] | [[Image:1i12.jpg|left|200px]] | ||
'''CRYSTAL STRUCTURE OF SACCHAROMYCES CEREVISIAE GNA1 COMPLEXED WITH ACCOA''' | {{Structure | ||
|PDB= 1i12 |SIZE=350|CAPTION= <scene name='initialview01'>1i12</scene>, resolution 1.30Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</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 SACCHAROMYCES CEREVISIAE GNA1 COMPLEXED WITH ACCOA''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1I12 is a [ | 1I12 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=1I12 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]] | [[Category: gnat]] | ||
''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 11:44:08 2008'' | ||
Revision as of 12:44, 20 March 2008
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| , resolution 1.30Å | |||||||
|---|---|---|---|---|---|---|---|
| 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 SACCHAROMYCES CEREVISIAE GNA1 COMPLEXED WITH ACCOA
OverviewOverview
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 StructureAbout this Structure
1I12 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
ReferenceReference
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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