Proteopedia

1wb5: Difference between revisions

New page: left|200px<br /> <applet load="1wb5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wb5, resolution 1.40Å" /> '''S954A MUTANT OF THE...
 
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[[Image:1wb5.gif|left|200px]]<br />
<applet load="1wb5" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1wb5, resolution 1.40&Aring;" />
'''S954A MUTANT OF THE FERULOYL ESTERASE MODULE FROM CLOSTRIDIUM THERMOCELLUM COMPLEXED WITH SYRINGATE'''<br />


==Overview==
==S954A mutant of the feruloyl esterase module from clostridium thermocellum complexed with syringate==
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, ... [[http://ispc.weizmann.ac.il/pmbin/getpm?15681871 (full description)]]
<StructureSection load='1wb5' size='340' side='right'caption='[[1wb5]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1wb5]] 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=1WB5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WB5 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]] 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=SYR:SYRINGATE'>SYR</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=1wb5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wb5 OCA], [https://pdbe.org/1wb5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wb5 RCSB], [https://www.ebi.ac.uk/pdbsum/1wb5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wb5 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/1wb5_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=1wb5 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.


==About this Structure==
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>
1WB5 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Clostridium_thermocellum Clostridium thermocellum]] with ACT, CD, SYR and GOL as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.8 3.2.1.8]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1WB5 OCA]].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15681871 15681871]
</div>
[[Category: Clostridium thermocellum]]
<div class="pdbe-citations 1wb5" style="background-color:#fffaf0;"></div>
[[Category: Single protein]]
== References ==
[[Category: Davies, G.J.]]
<references/>
[[Category: Fontes, C.]]
__TOC__
[[Category: Prates, J.A.]]
</StructureSection>
[[Category: Tarbouriech, N.]]
[[Category: Acetivibrio thermocellus]]
[[Category: ACT]]
[[Category: Large Structures]]
[[Category: CD]]
[[Category: Davies GJ]]
[[Category: GOL]]
[[Category: Fontes C]]
[[Category: SYR]]
[[Category: Prates JA]]
[[Category: esterase family 1]]
[[Category: Tarbouriech N]]
[[Category: ferulic acid]]
[[Category: glycosidase]]
[[Category: hydrolase]]
[[Category: repeat]]
[[Category: xylan degradation]]
[[Category: xylanase]]
 
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