1nyw: Difference between revisions

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 ==The high resolution structures of RmlC from Streptoccus suis in complex with dTDP-D-glucose==
-<StructureSection load='1nyw' size='340' side='right' caption='[[1nyw]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
+<StructureSection load='1nyw' size='340' side='right'caption='[[1nyw]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1nyw]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43765 Atcc 43765]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NYW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NYW FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1nyw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_suis Streptococcus suis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NYW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NYW FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DAU:2DEOXY-THYMIDINE-5-DIPHOSPHO-ALPHA-D-GLUCOSE'>DAU</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]] 1.6&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1nxm|1nxm]], [[1nzc|1nzc]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DAU:2DEOXY-THYMIDINE-5-DIPHOSPHO-ALPHA-D-GLUCOSE'>DAU</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rmlc ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1307 ATCC 43765])</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=1nyw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nyw OCA], [https://pdbe.org/1nyw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nyw RCSB], [https://www.ebi.ac.uk/pdbsum/1nyw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nyw ProSAT]</span></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/dTDP-4-dehydrorhamnose_3,5-epimerase dTDP-4-dehydrorhamnose 3,5-epimerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.1.3.13 5.1.3.13] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nyw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nyw OCA], [http://pdbe.org/1nyw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1nyw RCSB], [http://www.ebi.ac.uk/pdbsum/1nyw PDBsum]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q8GIQ0_STRSU Q8GIQ0_STRSU]
 == 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/ny/1nyw_consurf.spt"</scriptWhenChecked>
+     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ny/1nyw_consurf.spt"</scriptWhenChecked>
      <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
      <text>to colour the structure by Evolutionary Conservation</text>
@@ 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=1nyw ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Nature achieves the epimerization of carbohydrates by a variety of chemical routes. One common route is that performed by the class of enzyme defined by dTDP-6-deoxy-D-xylo-4-hexulose 3,5-epimerase (RmlC) from the rhamnose pathway. Earlier studies failed to identify the key residues in catalysis. We report the 1.3 A structure of RmlC from Streptococcus suis type 2 and its complexes with dTDP-D-glucose and dTDP-D-xylose. The streptococcal RmlC enzymes belong to a separate subgroup, sharing only 25% identity with RmlC from other bacteria, yet the S. suis enzyme has similar kinetic properties and structure to other RmlC enzymes. Structure, sequence alignment, and mutational analysis have now allowed reliable identification of the catalytic residues and their roles.
-High-resolution structures of RmlC from Streptococcus suis in complex with substrate analogs locate the active site of this class of enzyme.,Dong C, Major LL, Allen A, Blankenfeldt W, Maskell D, Naismith JH Structure. 2003 Jun;11(6):715-23. PMID:12791259<ref>PMID:12791259</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1nyw" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[RmlC|RmlC]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Atcc 43765]]
+[[Category: Large Structures]]
-[[Category: DTDP-4-dehydrorhamnose 3,5-epimerase]]
+[[Category: Streptococcus suis]]
-[[Category: Allen, A]]
+[[Category: Allen A]]
-[[Category: Blankenfeldt, W]]
+[[Category: Blankenfeldt W]]
-[[Category: Dong, C]]
+[[Category: Dong C]]
-[[Category: Major, L L]]
+[[Category: Major LL]]
-[[Category: Maskell, D]]
+[[Category: Maskell D]]
-[[Category: Naismith, J H]]
+[[Category: Naismith JH]]
-[[Category: Beta sheet]]
-[[Category: Isomerase]]
-[[Category: Jelly roll-like structure]]