1s3z

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{{Seed}}
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{{STRUCTURE_1s3z| PDB=1s3z | SCENE= }}
{{STRUCTURE_1s3z| PDB=1s3z | SCENE= }}
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'''Aminoglycoside N-Acetyltransferase AAC(6')-Iy in Complex with CoA and Ribostamycin'''
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===Aminoglycoside N-Acetyltransferase AAC(6')-Iy in Complex with CoA and Ribostamycin===
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==Overview==
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The Salmonella enterica chromosomally encoded AAC(6')-Iy has been shown to confer broad aminoglycoside resistance in strains in which the structural gene is expressed. The three-dimensional structures reported place the enzyme in the large Gcn5-related N-acetyltransferase (GNAT) superfamily. The structure of the CoA-ribostamycin ternary complex allows us to propose a chemical mechanism for the reaction, and comparison with the Mycobacterium tuberculosis AAC(2')-CoA-ribostamycin complex allows us to define how regioselectivity of acetylation is achieved. The AAC(6')-Iy dimer is most structurally similar to the Saccharomyces cerevisiae Hpa2-encoded histone acetyltransferase. We demonstrate that AAC(6')-Iy catalyzes both acetyl-CoA-dependent self-alpha-N-acetylation and acetylation of eukaryotic histone proteins and the human histone H3 N-terminal peptide. These structural and catalytic similarities lead us to propose that chromosomally encoded bacterial acetyltransferases, including those functionally identified as aminoglycoside acetyltransferases, are the evolutionary progenitors of the eukaryotic histone acetyltransferases.
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{{ABSTRACT_PUBMED_15123251}}
==About this Structure==
==About this Structure==
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[[Category: N-acetyltransferase]]
[[Category: N-acetyltransferase]]
[[Category: Ribostamycin]]
[[Category: Ribostamycin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:16:11 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 09:39:50 2008''

Revision as of 06:39, 28 July 2008

Image:1s3z.png

Template:STRUCTURE 1s3z

Aminoglycoside N-Acetyltransferase AAC(6')-Iy in Complex with CoA and Ribostamycin

Template:ABSTRACT PUBMED 15123251

About this Structure

1S3Z is a Single protein structure of sequence from Salmonella enteritidis. Full crystallographic information is available from OCA.

Reference

A bacterial acetyltransferase capable of regioselective N-acetylation of antibiotics and histones., Vetting MW, Magnet S, Nieves E, Roderick SL, Blanchard JS, Chem Biol. 2004 Apr;11(4):565-73. PMID:15123251

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