1s7l

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(New page: 200px<br /><applet load="1s7l" size="450" color="white" frame="true" align="right" spinBox="true" caption="1s7l, resolution 2.3&Aring;" /> '''RimL- Ribosomal L7/L1...)
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[[Image:1s7l.gif|left|200px]]<br /><applet load="1s7l" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1s7l, resolution 2.3&Aring;" />
 
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'''RimL- Ribosomal L7/L12 alpha-N-protein acetyltransferase in complex with Coenzyme A (CoA-Cys134 Disulfide)'''<br />
 
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==Overview==
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==RimL- Ribosomal L7/L12 alpha-N-protein acetyltransferase in complex with Coenzyme A (CoA-Cys134 Disulfide)==
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RimL is responsible for converting the prokaryotic ribosomal protein from, L12 to L7 by acetylation of its N-terminal amino group. We demonstrate, that purified RimL is capable of posttranslationally acetylating L12, exhibiting a V(max) of 21 min(-1). We have also determined the, apostructure of RimL from Salmonella typhimurium and its complex with, coenzyme A, revealing a homodimeric oligomer with structural similarity to, other Gcn5-related N-acetyltransferase superfamily members. A large, central trough located at the dimer interface provides sufficient room to, bind both L12 N-terminal helices. Structural and biochemical analysis, indicates that RimL proceeds by single-step transfer rather than a, covalent-enzyme intermediate. This is the first structure of a, Gcn5-related N-acetyltransferase family member with demonstrated activity, toward a protein N(alpha)-amino group and is a first step toward, understanding the molecular basis for N(alpha)acetylation and its function, in cellular regulation.
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<StructureSection load='1s7l' size='340' side='right'caption='[[1s7l]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1s7l]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium_str._LT2 Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S7L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1S7L FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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<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=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1s7l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s7l OCA], [https://pdbe.org/1s7l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1s7l RCSB], [https://www.ebi.ac.uk/pdbsum/1s7l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1s7l ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q8ZPC0_SALTY Q8ZPC0_SALTY]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/s7/1s7l_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1s7l ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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RimL is responsible for converting the prokaryotic ribosomal protein from L12 to L7 by acetylation of its N-terminal amino group. We demonstrate that purified RimL is capable of posttranslationally acetylating L12, exhibiting a V(max) of 21 min(-1). We have also determined the apostructure of RimL from Salmonella typhimurium and its complex with coenzyme A, revealing a homodimeric oligomer with structural similarity to other Gcn5-related N-acetyltransferase superfamily members. A large central trough located at the dimer interface provides sufficient room to bind both L12 N-terminal helices. Structural and biochemical analysis indicates that RimL proceeds by single-step transfer rather than a covalent-enzyme intermediate. This is the first structure of a Gcn5-related N-acetyltransferase family member with demonstrated activity toward a protein N(alpha)-amino group and is a first step toward understanding the molecular basis for N(alpha)acetylation and its function in cellular regulation.
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==About this Structure==
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A novel dimeric structure of the RimL Nalpha-acetyltransferase from Salmonella typhimurium.,Vetting MW, de Carvalho LP, Roderick SL, Blanchard JS J Biol Chem. 2005 Jun 10;280(23):22108-14. Epub 2005 Apr 6. PMID:15817456<ref>PMID:15817456</ref>
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1S7L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium_lt2 Salmonella typhimurium lt2] with SO4 and COA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1S7L OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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A novel dimeric structure of the RimL Nalpha-acetyltransferase from Salmonella typhimurium., Vetting MW, de Carvalho LP, Roderick SL, Blanchard JS, J Biol Chem. 2005 Jun 10;280(23):22108-14. Epub 2005 Apr 6. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15817456 15817456]
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</div>
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[[Category: Salmonella typhimurium lt2]]
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<div class="pdbe-citations 1s7l" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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== References ==
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[[Category: Blanchard, J.S.]]
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<references/>
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[[Category: Carvalho, L.P.de.]]
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__TOC__
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[[Category: Roderick, S.L.]]
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</StructureSection>
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[[Category: Vetting, M.W.]]
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[[Category: Large Structures]]
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[[Category: COA]]
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[[Category: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]]
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[[Category: SO4]]
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[[Category: Blanchard JS]]
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[[Category: acetyltransferase]]
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[[Category: Roderick SL]]
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[[Category: alpha-n-protein acetyltransferase]]
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[[Category: Vetting MW]]
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[[Category: coenzyme a]]
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[[Category: De Carvalho LP]]
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[[Category: gnat]]
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[[Category: l7/l12]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 00:02:43 2007''
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Current revision

RimL- Ribosomal L7/L12 alpha-N-protein acetyltransferase in complex with Coenzyme A (CoA-Cys134 Disulfide)

PDB ID 1s7l

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