1sqj
From Proteopedia
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| - | [[Image:1sqj.gif|left|200px]] | ||
| - | + | ==Crystal Structure Analysis of Oligoxyloglucan reducing-end-specific cellobiohydrolase (OXG-RCBH)== | |
| - | + | <StructureSection load='1sqj' size='340' side='right'caption='[[1sqj]], [[Resolution|resolution]] 2.20Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</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> | |
| - | | | + | == Function == |
| - | | | + | [https://www.uniprot.org/uniprot/CBHRE_GEOS1 CBHRE_GEOS1] |
| - | + | == 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/sq/1sqj_consurf.spt"</scriptWhenChecked> | |
| - | == | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1sqj ConSurf]. | ||
| + | <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. | 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> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1sqj" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Cellobiohydrolase 3D structures|Cellobiohydrolase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Geotrichum sp. M128]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Kondo H]] | ||
| + | [[Category: Mitsuishi Y]] | ||
| + | [[Category: Noro N]] | ||
| + | [[Category: Suzuki M]] | ||
| + | [[Category: Tsuda S]] | ||
| + | [[Category: Yaoi K]] | ||
Current revision
Crystal Structure Analysis of Oligoxyloglucan reducing-end-specific cellobiohydrolase (OXG-RCBH)
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Categories: Geotrichum sp. M128 | Large Structures | Kondo H | Mitsuishi Y | Noro N | Suzuki M | Tsuda S | Yaoi K
