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| | ==Crystal structure of Vibrio proteolyticus chitobiose phosphorylase== | | ==Crystal structure of Vibrio proteolyticus chitobiose phosphorylase== |
| - | <StructureSection load='1v7v' size='340' side='right' caption='[[1v7v]], [[Resolution|resolution]] 1.80Å' scene=''> | + | <StructureSection load='1v7v' size='340' side='right'caption='[[1v7v]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1v7v]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"aeromonas_proteolytica"_merkel_et_al._1964 "aeromonas proteolytica" merkel et al. 1964]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V7V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1V7V FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1v7v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_proteolyticus Vibrio proteolyticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V7V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1V7V FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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]] 1.8Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1v7w|1v7w]], [[1v7x|1v7x]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">chbp ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=671 "Aeromonas proteolytica" Merkel et al. 1964])</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=1v7v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v7v OCA], [https://pdbe.org/1v7v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1v7v RCSB], [https://www.ebi.ac.uk/pdbsum/1v7v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1v7v ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1v7v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v7v OCA], [http://pdbe.org/1v7v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1v7v RCSB], [http://www.ebi.ac.uk/pdbsum/1v7v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1v7v ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CHBP_VIBPR CHBP_VIBPR]] Catalyzes the reversible phosphorolysis of chitobiose (N,N'-diacetylchitobiose or (GlcNAc)(2)) into alpha-GlcNAc-1-phosphate and GlcNAc with inversion of the anomeric configuration.<ref>PMID:13678418</ref> | + | [https://www.uniprot.org/uniprot/CHBP_VIBPR CHBP_VIBPR] Catalyzes the reversible phosphorolysis of chitobiose (N,N'-diacetylchitobiose or (GlcNAc)(2)) into alpha-GlcNAc-1-phosphate and GlcNAc with inversion of the anomeric configuration.<ref>PMID:13678418</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Aeromonas proteolytica merkel et al. 1964]] | + | [[Category: Large Structures]] |
| - | [[Category: Fushinobu, S]] | + | [[Category: Vibrio proteolyticus]] |
| - | [[Category: Hayashi, K]] | + | [[Category: Fushinobu S]] |
| - | [[Category: Hidaka, M]] | + | [[Category: Hayashi K]] |
| - | [[Category: Honda, Y]] | + | [[Category: Hidaka M]] |
| - | [[Category: Kitaoka, M]] | + | [[Category: Honda Y]] |
| - | [[Category: Nirasawa, S]] | + | [[Category: Kitaoka M]] |
| - | [[Category: Shoun, H]] | + | [[Category: Nirasawa S]] |
| - | [[Category: Wakagi, T]] | + | [[Category: Shoun H]] |
| - | [[Category: Beta-sandwich]]
| + | [[Category: Wakagi T]] |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
CHBP_VIBPR Catalyzes the reversible phosphorolysis of chitobiose (N,N'-diacetylchitobiose or (GlcNAc)(2)) into alpha-GlcNAc-1-phosphate and GlcNAc with inversion of the anomeric configuration.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Vibrio proteolyticus chitobiose phosphorylase (ChBP) belongs to glycosyl transferase family 36 (GT-36), and catalyzes the reversible phosphorolysis of chitobiose into alpha-GlcNAc-1-phosphate and GlcNAc with inversion of the anomeric configuration. As the first known structures of a GT-36 enzyme, we determined the crystal structure of ChBP in a ternary complex with GlcNAc and SO(4). It is also the first structures of an inverting phosphorolytic enzyme in a complex with a sugar and a sulfate ion, and reveals a pseudo-ternary complex structure of enzyme-sugar-phosphate. ChBP comprises a beta sandwich domain and an (alpha/alpha)(6) barrel domain, constituting a distinctive structure among GT families. Instead, it shows significant structural similarity with glycoside hydrolase (GH) enzymes, glucoamylases (GH-15), and maltose phosphorylase (GH-65) in clan GH-L. The structural similarity reported here, together with distant sequence similarities between ChBP and GHs, led to the reclassification of family GT-36 into a novel GH family, namely GH-94.
Chitobiose phosphorylase from Vibrio proteolyticus, a member of glycosyl transferase family 36, has a clan GH-L-like (alpha/alpha)(6) barrel fold.,Hidaka M, Honda Y, Kitaoka M, Nirasawa S, Hayashi K, Wakagi T, Shoun H, Fushinobu S Structure. 2004 Jun;12(6):937-47. PMID:15274915[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Honda Y, Kitaoka M, Hayashi K. Reaction mechanism of chitobiose phosphorylase from Vibrio proteolyticus: identification of family 36 glycosyltransferase in Vibrio. Biochem J. 2004 Jan 1;377(Pt 1):225-32. PMID:13678418 doi:http://dx.doi.org/10.1042/BJ20031171
- ↑ Hidaka M, Honda Y, Kitaoka M, Nirasawa S, Hayashi K, Wakagi T, Shoun H, Fushinobu S. Chitobiose phosphorylase from Vibrio proteolyticus, a member of glycosyl transferase family 36, has a clan GH-L-like (alpha/alpha)(6) barrel fold. Structure. 2004 Jun;12(6):937-47. PMID:15274915 doi:10.1016/j.str.2004.03.027
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