1wb6: Difference between revisions

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-{{Seed}}
-[[Image:1wb6.png|left|200px]]
-<!--
+==S954A mutant of the feruloyl esterase module from clostridium thermocellum complexed with vanillate==
-The line below this paragraph, containing "STRUCTURE_1wb6", creates the "Structure Box" on the page.
+<StructureSection load='1wb6' size='340' side='right'caption='[[1wb6]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1wb6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Acetivibrio_thermocellus Acetivibrio thermocellus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WB6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WB6 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=VXX:METHYL+VANILLATE'>VXX</scene></td></tr>
-{{STRUCTURE_1wb6|  PDB=1wb6  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1wb6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wb6 OCA], [https://pdbe.org/1wb6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wb6 RCSB], [https://www.ebi.ac.uk/pdbsum/1wb6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wb6 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/XYNY_ACETH XYNY_ACETH]
+== 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/wb/1wb6_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=1wb6 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Feruloyl esterases play a key role in the degradation of the intricate structure of the plant cell wall by hydrolysing the ferulate ester groups involved in the cross-linking between hemicelluloses and between hemicellulose and lignin. The structure of the feruloyl esterase module of Clostridium thermocellum cellulosomal xylanase 10B has been reported previously. It displays the alpha/beta hydrolase fold with a classical Ser-His-Asp catalytic triad. Here, the structures of a Ser-Ala mutant of this feruloyl esterase in complexes with methyl syringate, methyl sinapinate and methyl vanillate are described. Substrate binding is accompanied by subtle conformational changes at amino acids Trp982, Met955, Asn1023 and Ile1019 in the ligand-binding cavity. The structural determinants, particularly the m-methoxy substituent, governing the substrate specificity of Xyn10B feruloyl esterase are rationalized.
-===S954A MUTANT OF THE FERULOYL ESTERASE MODULE FROM CLOSTRIDIUM THERMOCELLUM COMPLEXED WITH VANILLATE===
+Molecular determinants of substrate specificity in the feruloyl esterase module of xylanase 10B from Clostridium thermocellum.,Tarbouriech N, Prates JA, Fontes CM, Davies GJ Acta Crystallogr D Biol Crystallogr. 2005 Feb;61(Pt 2):194-7. Epub 2005, Jan 19. PMID:15681871<ref>PMID:15681871</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_15681871}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 1wb6" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 15681871 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_15681871}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Acetivibrio thermocellus]]
-WB6 is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Clostridium_thermocellum Clostridium thermocellum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WB6 OCA].
+[[Category: Large Structures]]
+[[Category: Davies GJ]]
-==Reference==
+[[Category: Fontes C]]
-<ref group="xtra">PMID:15681871</ref><references group="xtra"/>
+[[Category: Prates JA]]
-[[Category: Clostridium thermocellum]]
+[[Category: Tarbouriech N]]
-[[Category: Endo-1,4-beta-xylanase]]
-[[Category: Davies, G J.]]
-[[Category: Fontes, C.]]
-[[Category: Prates, J A.]]
-[[Category: Tarbouriech, N.]]
-[[Category: Esterase family 1]]
-[[Category: Ferulic acid]]
-[[Category: Glycosidase]]
-[[Category: Hydrolase]]
-[[Category: Repeat]]
-[[Category: Xylan degradation]]
-[[Category: Xylanase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 04:22:26 2009''