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<StructureSection load='1sqj' size='340' side='right'caption='[[1sqj]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='1sqj' size='340' side='right'caption='[[1sqj]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1sqj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Geos1 Geos1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SQJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SQJ FirstGlance]. <br>
<table><tr><td colspan='2'>[[1sqj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Geotrichum_sp._M128 Geotrichum sp. M128]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SQJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SQJ FirstGlance]. <br>
</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Oligoxyloglucan_reducing-end-specific_cellobiohydrolase Oligoxyloglucan reducing-end-specific cellobiohydrolase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.150 3.2.1.150] </span></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]] 2.2&#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=1sqj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sqj OCA], [https://pdbe.org/1sqj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sqj RCSB], [https://www.ebi.ac.uk/pdbsum/1sqj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sqj 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=1sqj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sqj OCA], [https://pdbe.org/1sqj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sqj RCSB], [https://www.ebi.ac.uk/pdbsum/1sqj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sqj ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CBHRE_GEOS1 CBHRE_GEOS1]
== 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=1sqj 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=1sqj ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Oligoxyloglucan reducing-end-specific cellobiohydrolase (OXG-RCBH; EC 3.2.1.150) is an exoglucanase that recognizes the reducing end of oligoxyloglucan and releases two glucosyl residue segments from the main chain. The X-ray crystal structure of OXG-RCBH determined at 2.2 A resolution reveals a unique feature of this enzyme; OXG-RCBH consists of a tandem repeat of two similar domains, which are both folded into seven-bladed beta-propeller structures. The sequence alignment of the propeller blades, based on the structure, indicates that a weak repeat of the amino acid sequence occurred seven times to construct each domain. There is a cleft that can accommodate the substrate oligosaccharide between the two domains, which is a putative substrate binding subsite. Mutation of either Asp35 or Asp465, located in the putative catalytic center, to Asn resulted in a protein with no detectable catalytic activity, indicating the critical role of these amino acids in catalysis.
Tandem repeat of a seven-bladed beta-propeller domain in oligoxyloglucan reducing-end-specific cellobiohydrolase.,Yaoi K, Kondo H, Noro N, Suzuki M, Tsuda S, Mitsuishi Y Structure. 2004 Jul;12(7):1209-17. PMID:15242597<ref>PMID:15242597</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1sqj" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Cellobiohydrolase 3D structures|Cellobiohydrolase 3D structures]]
*[[Cellobiohydrolase 3D structures|Cellobiohydrolase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Geos1]]
[[Category: Geotrichum sp. M128]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Oligoxyloglucan reducing-end-specific cellobiohydrolase]]
[[Category: Kondo H]]
[[Category: Kondo, H]]
[[Category: Mitsuishi Y]]
[[Category: Mitsuishi, Y]]
[[Category: Noro N]]
[[Category: Noro, N]]
[[Category: Suzuki M]]
[[Category: Suzuki, M]]
[[Category: Tsuda S]]
[[Category: Tsuda, S]]
[[Category: Yaoi K]]
[[Category: Yaoi, K]]
[[Category: Beta-propeller]]
[[Category: Hydrolase]]
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