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2cnm
From Proteopedia
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| - | [[Image:2cnm.gif|left|200px]]<br /> | ||
| - | <applet load="2cnm" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2cnm, resolution 2.60Å" /> | ||
| - | '''RIMI- RIBOSOMAL S18 N-ALPHA-PROTEIN ACETYLTRANSFERASE IN COMPLEX WITH A BISUBSTRATE INHIBITOR (CTERM-ARG-ARG-PHE-TYR-ARG-ALA-N-ALPHA-ACETYL-S-COA).'''<br /> | ||
| - | == | + | ==RimI - Ribosomal S18 N-alpha-protein acetyltransferase in complex with a bisubstrate inhibitor (Cterm-Arg-Arg-Phe-Tyr-Arg-Ala-N-alpha- acetyl-S-CoA).== |
| - | + | <StructureSection load='2cnm' size='340' side='right'caption='[[2cnm]], [[Resolution|resolution]] 2.60Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[2cnm]] is a 6 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=2CNM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CNM FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</td></tr> | |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <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=2cnm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cnm OCA], [https://pdbe.org/2cnm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cnm RCSB], [https://www.ebi.ac.uk/pdbsum/2cnm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cnm ProSAT]</span></td></tr> | |
| - | [ | + | </table> |
| - | [ | + | == Function == |
| - | [[ | + | [https://www.uniprot.org/uniprot/RIMI_SALTY RIMI_SALTY] Acetylates the N-terminal alanine of ribosomal protein S18.[HAMAP-Rule:MF_02210]<ref>PMID:18596200</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/cn/2cnm_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=2cnm ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The three ribosomal proteins L7, S5, and S18 are included in the rare subset of prokaryotic proteins that are known to be N(alpha)-acetylated. The GCN5-related N-acetyltransferase (GNAT) protein RimI, responsible for the N(alpha)-acetylation of the ribosomal protein S18, was cloned from Salmonella typhimurium LT2 (RimI(ST)), overexpressed, and purified to homogeneity. Steady-state kinetic parameters for RimI(ST) were determined for AcCoA and a peptide substrate consisting of the first six amino acids of the target protein S18. The crystal structure of RimI(ST) was determined in complex with CoA, AcCoA, and a CoA-S-acetyl-ARYFRR bisubstrate inhibitor. The structures are consistent with a direct nucleophilic addition-elimination mechanism with Glu103 and Tyr115 acting as the catalytic base and acid, respectively. The RimI(ST)-bisubstrate complex suggests that several residues change conformation upon interacting with the N terminus of S18, including Glu103, the proposed active site base, facilitating proton exchange and catalysis. | ||
| - | + | Crystal structure of RimI from Salmonella typhimurium LT2, the GNAT responsible for N(alpha)-acetylation of ribosomal protein S18.,Vetting MW, Bareich DC, Yu M, Blanchard JS Protein Sci. 2008 Oct;17(10):1781-90. Epub 2008 Jul 2. PMID:18596200<ref>PMID:18596200</ref> | |
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 2cnm" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Ribosomal protein S18|Ribosomal protein S18]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]] | ||
| + | [[Category: Bareich DC]] | ||
| + | [[Category: Blanchard JS]] | ||
| + | [[Category: Vetting MW]] | ||
| + | [[Category: Yu M]] | ||
Current revision
RimI - Ribosomal S18 N-alpha-protein acetyltransferase in complex with a bisubstrate inhibitor (Cterm-Arg-Arg-Phe-Tyr-Arg-Ala-N-alpha- acetyl-S-CoA).
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