1s3z
From Proteopedia
(Difference between revisions)
| (12 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | [[Image:1s3z.gif|left|200px]] | ||
| - | + | ==Aminoglycoside N-Acetyltransferase AAC(6')-Iy in Complex with CoA and Ribostamycin== | |
| - | + | <StructureSection load='1s3z' size='340' side='right'caption='[[1s3z]], [[Resolution|resolution]] 2.00Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | | | + | <table><tr><td colspan='2'>[[1s3z]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S3Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1S3Z FirstGlance]. <br> |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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></td></tr> | |
| - | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Aminoglycoside_N(6')-acetyltransferase Aminoglycoside N(6')-acetyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.82 2.3.1.82] </span></td></tr> | |
| - | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1s3z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s3z OCA], [https://pdbe.org/1s3z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1s3z RCSB], [https://www.ebi.ac.uk/pdbsum/1s3z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1s3z ProSAT]</span></td></tr> | |
| - | + | </table> | |
| - | + | == Function == | |
| - | + | [[https://www.uniprot.org/uniprot/AAC6_SALEN AAC6_SALEN]] Catalyzes the transfer of an acetyl group from acetyl-CoA to the 6'-amino group of aminoglycoside molecules conferring resistance to antibiotics containing the purpurosamine ring including amikacin, tobramycin, dibekacin and ribostamycin. Able to acetylate eukaryotic histone proteins.<ref>PMID:10542165</ref> <ref>PMID:15123251</ref> | |
| - | + | == Evolutionary Conservation == | |
| - | + | [[Image:Consurf_key_small.gif|200px|right]] | |
| - | + | Check<jmol> | |
| - | + | <jmolCheckbox> | |
| - | == | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/s3/1s3z_consurf.spt"</scriptWhenChecked> |
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1s3z ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
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. | 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. | ||
| - | + | 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<ref>PMID:15123251</ref> | |
| - | + | ||
| - | + | ||
| - | + | ||
| - | A bacterial acetyltransferase capable of regioselective N-acetylation of antibiotics and histones., Vetting MW, Magnet S, Nieves E, Roderick SL, Blanchard JS | + | |
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 1s3z" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Blachard, J S]] | ||
| + | [[Category: Magnet, S]] | ||
| + | [[Category: Nieves, E]] | ||
| + | [[Category: Roderick, S L]] | ||
| + | [[Category: Vetting, M W]] | ||
| + | [[Category: Acetyltransferase]] | ||
| + | [[Category: Aminoglycoside]] | ||
| + | [[Category: Coa]] | ||
| + | [[Category: Gnat]] | ||
| + | [[Category: N-acetyltransferase]] | ||
| + | [[Category: Ribostamycin]] | ||
| + | [[Category: Transferase]] | ||
Current revision
Aminoglycoside N-Acetyltransferase AAC(6')-Iy in Complex with CoA and Ribostamycin
| |||||||||||
