1s60: Difference between revisions
New page: left|200px<br /><applet load="1s60" size="450" color="white" frame="true" align="right" spinBox="true" caption="1s60, resolution 3.0Å" /> '''Aminoglycoside N-Acet... |
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[[Image:1s60.jpg|left|200px]]<br /><applet load="1s60" size=" | [[Image:1s60.jpg|left|200px]]<br /><applet load="1s60" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1s60, resolution 3.0Å" /> | caption="1s60, resolution 3.0Å" /> | ||
'''Aminoglycoside N-Acetyltransferase AAC(6')-Iy in Complex with CoA and N-terminal His(6)-tag (crystal form 2)'''<br /> | '''Aminoglycoside N-Acetyltransferase AAC(6')-Iy in Complex with CoA and N-terminal His(6)-tag (crystal form 2)'''<br /> | ||
==Overview== | ==Overview== | ||
The Salmonella enterica chromosomally encoded AAC(6')-Iy has been shown to | 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== | ==About this Structure== | ||
1S60 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_enteritidis Salmonella enteritidis] with SO4 and COA as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http:// | 1S60 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_enteritidis Salmonella enteritidis] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=COA:'>COA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S60 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Salmonella enteritidis]] | [[Category: Salmonella enteritidis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Blanchard, J | [[Category: Blanchard, J S.]] | ||
[[Category: Magnet, S.]] | [[Category: Magnet, S.]] | ||
[[Category: Nieves, E.]] | [[Category: Nieves, E.]] | ||
[[Category: Roderick, S | [[Category: Roderick, S L.]] | ||
[[Category: Vetting, M | [[Category: Vetting, M W.]] | ||
[[Category: COA]] | [[Category: COA]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
| Line 27: | Line 27: | ||
[[Category: n-acetyltransferase]] | [[Category: n-acetyltransferase]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:58:25 2008'' | ||
Revision as of 15:58, 21 February 2008
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Aminoglycoside N-Acetyltransferase AAC(6')-Iy in Complex with CoA and N-terminal His(6)-tag (crystal form 2)
OverviewOverview
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 StructureAbout this Structure
1S60 is a Single protein structure of sequence from Salmonella enteritidis with and as ligands. Active as Aminoglycoside N(6')-acetyltransferase, with EC number 2.3.1.82 Full crystallographic information is available from OCA.
ReferenceReference
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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