1azw: Difference between revisions

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 ==PROLINE IMINOPEPTIDASE FROM XANTHOMONAS CAMPESTRIS PV. CITRI==
-<StructureSection load='1azw' size='340' side='right' caption='[[1azw]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
+<StructureSection load='1azw' size='340' side='right'caption='[[1azw]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1azw]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"xanthomonas_citri"_(hasse_1915)_dowson_1939 "xanthomonas citri" (hasse 1915) dowson 1939]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AZW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AZW FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1azw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Xanthomonas_citri Xanthomonas citri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AZW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AZW FirstGlance]. <br>
-</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Prolyl_aminopeptidase Prolyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.5 3.4.11.5] </span></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]] 2.7&#8491;</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=1azw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1azw OCA], [http://pdbe.org/1azw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1azw RCSB], [http://www.ebi.ac.uk/pdbsum/1azw PDBsum]</span></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=1azw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1azw OCA], [https://pdbe.org/1azw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1azw RCSB], [https://www.ebi.ac.uk/pdbsum/1azw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1azw ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/PIP_XANCI PIP_XANCI]] May be involved in proline metabolism and sensitivity to ascamycin. Has ascamycin dealanylating activity.
+[https://www.uniprot.org/uniprot/PIP_XANCI PIP_XANCI] May be involved in proline metabolism and sensitivity to ascamycin. Has ascamycin dealanylating activity.
 == 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/az/1azw_consurf.spt"</scriptWhenChecked>
+     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/az/1azw_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/chain_selection.php?pdb_ID=2ata ConSurf].
+</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=1azw ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The proline iminopeptidase from Xanthomonas campestris pv. citri is a serine peptidase that catalyses the removal of N-terminal proline residues from peptides with high specificity. We have solved its three-dimensional structure by multiple isomorphous replacement and refined it to a crystallographic R-factor of 19.2% using X-ray data to 2.7 A resolution. The protein is folded into two contiguous domains. The larger domain shows the general topology of the alpha/beta hydrolase fold, with a central eight-stranded beta-sheet flanked by two helices and the 11 N-terminal residues on one side, and by four helices on the other side. The smaller domain is placed on top of the larger domain and essentially consists of six helices. The active site, located at the end of a deep pocket at the interface between both domains, includes a catalytic triad of Ser110, Asp266 and His294. Cys269, located at the bottom of the active site very close to the catalytic triad, presumably accounts for the inhibition by thiol-specific reagents. The overall topology of this iminopeptidase is very similar to that of yeast serine carboxypeptidase. The striking secondary structure similarity to human lymphocytic prolyl oligopeptidase and dipeptidyl peptidase IV makes this proline iminopeptidase structure a suitable model for the three-dimensional structure of other peptidases of this family.
-Structure of proline iminopeptidase from Xanthomonas campestris pv. citri: a prototype for the prolyl oligopeptidase family.,Medrano FJ, Alonso J, Garcia JL, Romero A, Bode W, Gomis-Ruth FX EMBO J. 1998 Jan 2;17(1):1-9. PMID:9427736<ref>PMID:9427736</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1azw" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Prolyl aminopeptidase]]
+[[Category: Large Structures]]
-[[Category: Alonso, J]]
+[[Category: Xanthomonas citri]]
-[[Category: Bode, W]]
+[[Category: Alonso J]]
-[[Category: Garcia, J L]]
+[[Category: Bode W]]
-[[Category: Gomis-Ruth, F X]]
+[[Category: Garcia JL]]
-[[Category: Medrano, F J]]
+[[Category: Gomis-Ruth FX]]
-[[Category: Romero, A]]
+[[Category: Medrano FJ]]
-[[Category: Aminopeptidase]]
+[[Category: Romero A]]
-[[Category: Proline iminopeptidase]]
-[[Category: Serine protease]]
-[[Category: Xanthomonas campestri]]