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3acs

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Current revision (14:18, 1 November 2023) (edit) (undo)
 
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<StructureSection load='3acs' size='340' side='right'caption='[[3acs]], [[Resolution|resolution]] 2.51&Aring;' scene=''>
<StructureSection load='3acs' size='340' side='right'caption='[[3acs]], [[Resolution|resolution]] 2.51&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3acs]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Celga Celga]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ACS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ACS FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3acs]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Cellulomonas_gilvus_ATCC_13127 Cellulomonas gilvus ATCC 13127]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ACS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ACS FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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]] 2.51&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2cqs|2cqs]], [[2cqt|2cqt]], [[3act|3act]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Cellobiose_phosphorylase Cellobiose phosphorylase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.20 2.4.1.20] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3acs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3acs OCA], [https://pdbe.org/3acs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3acs RCSB], [https://www.ebi.ac.uk/pdbsum/3acs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3acs 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=3acs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3acs OCA], [https://pdbe.org/3acs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3acs RCSB], [https://www.ebi.ac.uk/pdbsum/3acs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3acs ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/O66264_9CELL O66264_9CELL]
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Cellobiose phosphorylase, a member of the glycoside hydrolase family 94, catalyses the reversible phosphorolysis of cellobiose into alpha-D-glucose 1-phosphate and D-glucose with inversion of the anomeric configuration. The substrate specificity and reaction mechanism of cellobiose phosphorylase from Cellvibrio gilvus have been investigated in detail. We have determined the crystal structure of the glucose-sulphate and glucose-phosphate complexes of this enzyme at a maximal resolution of 2.0 A (1 A=0.1 nm). The phosphate ion is strongly held through several hydrogen bonds, and the configuration appears to be suitable for direct nucleophilic attack to an anomeric centre. Structural features around the sugar-donor and sugar-acceptor sites were consistent with the results of extensive kinetic studies. When we compared this structure with that of homologous chitobiose phosphorylase, we identified key residues for substrate discrimination between glucose and N-acetylglucosamine in both the sugar-donor and sugar-acceptor sites. We found that the active site pocket of cellobiose phosphorylase was covered by an additional loop, indicating that some conformational change is required upon substrate binding. Information on the three-dimensional structure of cellobiose phosphorylase will facilitate engineering of this enzyme, the application of which to practical oligosaccharide synthesis has already been established.
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Structural dissection of the reaction mechanism of cellobiose phosphorylase.,Hidaka M, Kitaoka M, Hayashi K, Wakagi T, Shoun H, Fushinobu S Biochem J. 2006 Aug 15;398(1):37-43. PMID:16646954<ref>PMID:16646954</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 3acs" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Celga]]
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[[Category: Cellulomonas gilvus ATCC 13127]]
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[[Category: Cellobiose phosphorylase]]
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[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Arai, T]]
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[[Category: Arai T]]
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[[Category: Fushinobu, S]]
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[[Category: Fushinobu S]]
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[[Category: Hidaka, M]]
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[[Category: Hidaka M]]
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[[Category: Beta-sandwich]]
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[[Category: Glycoside hydrolase family 94]]
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[[Category: Phosphorylase]]
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[[Category: Transferase]]
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Current revision

Crystal Structure of Cellvibrio gilvus Cellobiose Phosphorylase W488F mutant

PDB ID 3acs

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