1xyz

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Current revision (08:54, 14 February 2024) (edit) (undo)
 
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<StructureSection load='1xyz' size='340' side='right'caption='[[1xyz]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
<StructureSection load='1xyz' size='340' side='right'caption='[[1xyz]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1xyz]] is a 2 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=1XYZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XYZ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1xyz]] 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=1XYZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XYZ FirstGlance]. <br>
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</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Endo-1,4-beta-xylanase Endo-1,4-beta-xylanase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.8 3.2.1.8] </span></td></tr>
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</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1xyz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xyz OCA], [https://pdbe.org/1xyz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xyz RCSB], [https://www.ebi.ac.uk/pdbsum/1xyz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xyz ProSAT]</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=1xyz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xyz OCA], [https://pdbe.org/1xyz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xyz RCSB], [https://www.ebi.ac.uk/pdbsum/1xyz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xyz ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/XYNZ_ACET2 XYNZ_ACET2]
== 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=1xyz 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=1xyz ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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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.
 
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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>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 1xyz" style="background-color:#fffaf0;"></div>
 
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Ruminiclostridium thermocellum yutin and galperin 2013]]
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[[Category: Acetivibrio thermocellus]]
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[[Category: Endo-1,4-beta-xylanase]]
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[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Alzari, P M]]
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[[Category: Alzari PM]]
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[[Category: Dominguez, R]]
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[[Category: Dominguez R]]
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[[Category: Spinelli, S]]
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[[Category: Spinelli S]]
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[[Category: Clostridium thermocellum]]
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[[Category: Family f/10 of glycosyl hydrolase]]
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[[Category: Glycosyl hydrolase]]
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[[Category: Glycosyltransferase]]
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[[Category: Xylanase]]
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Current revision

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

PDB ID 1xyz

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