1s7n: Difference between revisions
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<StructureSection load='1s7n' size='340' side='right'caption='[[1s7n]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='1s7n' size='340' side='right'caption='[[1s7n]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1s7n]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1s7n]] is a 4 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=1S7N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1S7N FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene></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=1s7n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s7n OCA], [https://pdbe.org/1s7n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1s7n RCSB], [https://www.ebi.ac.uk/pdbsum/1s7n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1s7n ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q8ZPC0_SALTY Q8ZPC0_SALTY] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]] | ||
[[Category: Blanchard | [[Category: Blanchard JS]] | ||
[[Category: Roderick SL]] | |||
[[Category: Roderick | [[Category: Vetting MW]] | ||
[[Category: Vetting | [[Category: De Carvalho LP]] | ||
[[Category: | |||
Latest revision as of 09:13, 23 August 2023
Ribosomal L7/L12 alpha-N-protein acetyltransferase in complex with Coenzyme A (CoA free sulfhydryl)Ribosomal L7/L12 alpha-N-protein acetyltransferase in complex with Coenzyme A (CoA free sulfhydryl)
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedRimL 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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