1s3z
From Proteopedia
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|PDB= 1s3z |SIZE=350|CAPTION= <scene name='initialview01'>1s3z</scene>, resolution 2.00Å | |PDB= 1s3z |SIZE=350|CAPTION= <scene name='initialview01'>1s3z</scene>, resolution 2.00Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=RIO:RIBOSTAMYCIN'>RIO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Aminoglycoside_N(6')-acetyltransferase Aminoglycoside N(6')-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.82 2.3.1.82] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Aminoglycoside_N(6')-acetyltransferase Aminoglycoside N(6')-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.82 2.3.1.82] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1s3z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s3z OCA], [http://www.ebi.ac.uk/pdbsum/1s3z PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1s3z RCSB]</span> | ||
}} | }} | ||
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[[Category: Roderick, S L.]] | [[Category: Roderick, S L.]] | ||
[[Category: Vetting, M W.]] | [[Category: Vetting, M W.]] | ||
| - | [[Category: COA]] | ||
| - | [[Category: NI]] | ||
| - | [[Category: RIO]] | ||
| - | [[Category: SO4]] | ||
[[Category: acetyltransferase]] | [[Category: acetyltransferase]] | ||
[[Category: aminoglycoside]] | [[Category: aminoglycoside]] | ||
| Line 39: | Line 38: | ||
[[Category: ribostamycin]] | [[Category: ribostamycin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:36:59 2008'' |
Revision as of 20:37, 30 March 2008
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| , resolution 2.00Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Activity: | Aminoglycoside N(6')-acetyltransferase, with EC number 2.3.1.82 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Aminoglycoside N-Acetyltransferase AAC(6')-Iy in Complex with CoA and Ribostamycin
Overview
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.
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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