View source for 2vpt


==Clostridium thermocellum family 3 carbohydrate esterase==
<StructureSection load='2vpt' size='340' side='right'caption='[[2vpt]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2vpt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"ruminiclostridium_thermocellum"_yutin_and_galperin_2013 "ruminiclostridium thermocellum" yutin and galperin 2013]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VPT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VPT FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Acetylxylan_esterase Acetylxylan esterase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.72 3.1.1.72] </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=2vpt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vpt OCA], [https://pdbe.org/2vpt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vpt RCSB], [https://www.ebi.ac.uk/pdbsum/2vpt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vpt ProSAT]</span></td></tr>
</table>
== 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/vp/2vpt_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=2vpt ConSurf].
<div style="clear:both"></div>
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== Publication Abstract from PubMed ==
The microbial degradation of the plant cell wall is of increasing industrial significance, exemplified by the interest in generating biofuels from plant cell walls. The majority of plant cell-wall polysaccharides are acetylated, and removal of the acetyl groups through the action of carbohydrate esterases greatly increases the efficiency of polysaccharide saccharification. Enzymes in carbohydrate esterase family 3 (CE3) are common in plant cell wall-degrading microorganisms but there is a paucity of structural and biochemical information on these biocatalysts. Clostridium thermocellum contains a single CE3 enzyme, CtCes3, which comprises two highly homologous (97% sequence identity) catalytic modules appended to a C-terminal type I dockerin that targets the esterase into the cellulosome, a large protein complex that catalyses plant cell wall degradation. Here, we report the crystal structure and biochemical properties of the N-terminal catalytic module (CtCes3-1) of CtCes3. The enzyme is a thermostable acetyl-specific esterase that exhibits a strong preference for acetylated xylan. CtCes3-1 displays an alpha/beta hydrolase fold that contains a central five-stranded parallel twisted beta-sheet flanked by six alpha-helices. In addition, the enzyme contains a canonical catalytic triad in which Ser44 is the nucleophile, His208 is the acid-base and Asp205 modulates the basic nature of the histidine. The acetate moiety is accommodated in a hydrophobic pocket and the negative charge of the tetrahedral transition state is stabilized through hydrogen bonds with the backbone N of Ser44 and Gly95 and the side-chain amide of Asn124.

Crystal structure of a cellulosomal family 3 carbohydrate esterase from Clostridium thermocellum provides insights into the mechanism of substrate recognition.,Correia MA, Prates JA, Bras J, Fontes CM, Newman JA, Lewis RJ, Gilbert HJ, Flint JE J Mol Biol. 2008 May 23;379(1):64-72. Epub 2008 Mar 28. PMID:18436237<ref>PMID:18436237</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 2vpt" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Ruminiclostridium thermocellum yutin and galperin 2013]]
[[Category: Acetylxylan esterase]]
[[Category: Large Structures]]
[[Category: Bras, J]]
[[Category: Correia, M A.S]]
[[Category: Flint, J E]]
[[Category: Fontes, C M.G A]]
[[Category: Gilbert, H J]]
[[Category: Lewis, R J]]
[[Category: Newman, J A]]
[[Category: Prates, J A.M]]
[[Category: Esterase]]
[[Category: Hydrolase]]