1i12: Difference between revisions

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|PDB= 1i12 |SIZE=350|CAPTION= <scene name='initialview01'>1i12</scene>, resolution 1.30&Aring;
|PDB= 1i12 |SIZE=350|CAPTION= <scene name='initialview01'>1i12</scene>, resolution 1.30&Aring;
|SITE=  
|SITE=  
|LIGAND= <scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene> and <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>
|LIGAND= <scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene>, <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]  
|ACTIVITY= <span class='plainlinks'>[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] </span>
|GENE= YFL017C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
|GENE= YFL017C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
|DOMAIN=
|RELATEDENTRY=[[1i1d|1I1D]], [[1i21|1I21]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1i12 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i12 OCA], [http://www.ebi.ac.uk/pdbsum/1i12 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1i12 RCSB]</span>
}}
}}


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[[Category: Mengin-Lecreulx, D.]]
[[Category: Mengin-Lecreulx, D.]]
[[Category: Peneff, C.]]
[[Category: Peneff, C.]]
[[Category: ACO]]
[[Category: IMD]]
[[Category: alpha/beta]]
[[Category: alpha/beta]]
[[Category: gnat]]
[[Category: gnat]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:44:08 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:13:09 2008''

Revision as of 21:13, 30 March 2008

File:1i12.jpg


PDB ID 1i12

Drag the structure with the mouse to rotate
, resolution 1.30Å
Ligands: ,
Gene: YFL017C (Saccharomyces cerevisiae)
Activity: Glucosamine 6-phosphate N-acetyltransferase, with EC number 2.3.1.4
Related: 1I1D, 1I21


Resources: FirstGlance, OCA, PDBsum, RCSB
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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