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<StructureSection load='1cec' size='340' side='right'caption='[[1cec]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
<StructureSection load='1cec' size='340' side='right'caption='[[1cec]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1cec]] is a 1 chain structure with sequence from [http://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=1CEC OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1CEC FirstGlance]. <br>
<table><tr><td colspan='2'>[[1cec]] is a 1 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=1CEC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CEC FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MC1061 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1515 "Ruminiclostridium thermocellum" Yutin and Galperin 2013])</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]] 2.15&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cellulase Cellulase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4] </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=1cec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cec OCA], [https://pdbe.org/1cec PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cec RCSB], [https://www.ebi.ac.uk/pdbsum/1cec PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cec ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1cec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cec OCA], [http://pdbe.org/1cec PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1cec RCSB], [http://www.ebi.ac.uk/pdbsum/1cec PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1cec ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/GUNC_CLOTM GUNC_CLOTM]] This enzyme catalyzes the endohydrolysis of 1,4-beta-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.  
[https://www.uniprot.org/uniprot/GUNC_ACETH GUNC_ACETH] This enzyme catalyzes the endohydrolysis of 1,4-beta-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=1cec 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=1cec ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The structure of Clostridium thermocellum endoglucanase CelC, a member of the largest cellulase family (family A), has been determined at 2.15 A resolution. The protein folds into an (alpha/beta)8 barrel, with a deep active-site cleft generated by the insertion of a helical subdomain. The structure of the catalytic core of xylanase XynZ, which belongs to xylanase family F, has been determined at 1.4 A resolution. In spite of significant differences in substrate specificity and structure (including the absence of the helical subdomain), the general polypeptide folding pattern, architecture of the active site and catalytic mechanism of XynZ and CelC are similar, suggesting a common evolutionary origin.
A common protein fold and similar active site in two distinct families of beta-glycanases.,Dominguez R, Souchon H, Spinelli S, Dauter Z, Wilson KS, Chauvaux S, Beguin P, Alzari PM Nat Struct Biol. 1995 Jul;2(7):569-76. PMID:7664125<ref>PMID:7664125</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1cec" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Glucanase 3D structures|Glucanase 3D structures]]
*[[Glucanase 3D structures|Glucanase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Ruminiclostridium thermocellum yutin and galperin 2013]]
[[Category: Acetivibrio thermocellus]]
[[Category: Cellulase]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Alzari, P M]]
[[Category: Alzari PM]]
[[Category: Dominguez, R]]
[[Category: Dominguez R]]
[[Category: Clostridium thermocellum]]
[[Category: Endoglucanase c]]
[[Category: Family a/5 of cellulases/glycosyl hydrolase]]
[[Category: Glycosyl hydrolase]]

Latest revision as of 06:42, 7 February 2024

A COMMON PROTEIN FOLD AND SIMILAR ACTIVE SITE IN TWO DISTINCT FAMILIES OF BETA-GLYCANASES

1cec, resolution 2.15Å

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