1s7f: Difference between revisions

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 <StructureSection load='1s7f' size='340' side='right'caption='[[1s7f]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1s7f]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Salty Salty]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S7F OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1S7F FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1s7f]] 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=1S7F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1S7F FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MLA:MALONIC+ACID'>MLA</scene></td></tr>
+</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&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1s7k|1s7k]], [[1s7l|1s7l]], [[1s7n|1s7n]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MLA:MALONIC+ACID'>MLA</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RimL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=99287 SALTY])</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=1s7f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s7f OCA], [https://pdbe.org/1s7f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1s7f RCSB], [https://www.ebi.ac.uk/pdbsum/1s7f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1s7f ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1s7f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s7f OCA], [http://pdbe.org/1s7f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1s7f RCSB], [http://www.ebi.ac.uk/pdbsum/1s7f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1s7f ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q8ZPC0_SALTY Q8ZPC0_SALTY]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 19: / Line 20: @@
 </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=1s7f ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-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.
-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>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1s7f" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Salty]]
+[[Category: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]]
-[[Category: Blanchard, J S]]
+[[Category: Blanchard JS]]
-[[Category: Carvalho, L P.de]]
+[[Category: Roderick SL]]
-[[Category: Roderick, S L]]
+[[Category: Vetting MW]]
-[[Category: Vetting, M W]]
+[[Category: De Carvalho LP]]
-[[Category: Acetyltransferase]]
-[[Category: Alpha-n-protein acetyltransferase]]
-[[Category: Coenzyme some]]
-[[Category: Gnat]]
-[[Category: L7/l12]]
-[[Category: Transferase]]