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| | <StructureSection load='5b0q' size='340' side='right'caption='[[5b0q]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='5b0q' size='340' side='right'caption='[[5b0q]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5b0q]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lisin Lisin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5B0Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5B0Q FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5b0q]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Listeria_innocua_Clip11262 Listeria innocua Clip11262]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5B0Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5B0Q FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5b0p|5b0p]], [[5b0r|5b0r]], [[5b0s|5b0s]]</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=5b0q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b0q OCA], [https://pdbe.org/5b0q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5b0q RCSB], [https://www.ebi.ac.uk/pdbsum/5b0q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5b0q ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lin0857 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272626 LISIN])</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=5b0q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b0q OCA], [http://pdbe.org/5b0q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5b0q RCSB], [http://www.ebi.ac.uk/pdbsum/5b0q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5b0q ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/BMBP_LISIN BMBP_LISIN] Catalyzes the reversible phosphorolysis of 1,2-beta-oligomannan (PubMed:26632508). In phosphorolytic reactions, prefers beta-1,2-mannobiose (beta-1,2-Man2) as substrate, but can also use beta-1,2-mannotriose (PubMed:26632508).<ref>PMID:26632508</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lisin]] | + | [[Category: Listeria innocua Clip11262]] |
| - | [[Category: Arakawa, T]] | + | [[Category: Arakawa T]] |
| - | [[Category: Fushinobu, S]] | + | [[Category: Fushinobu S]] |
| - | [[Category: Tsuda, T]] | + | [[Category: Tsuda T]] |
| - | [[Category: Glycoside phosphorylase]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
BMBP_LISIN Catalyzes the reversible phosphorolysis of 1,2-beta-oligomannan (PubMed:26632508). In phosphorolytic reactions, prefers beta-1,2-mannobiose (beta-1,2-Man2) as substrate, but can also use beta-1,2-mannotriose (PubMed:26632508).[1]
Publication Abstract from PubMed
Glycoside hydrolase family 130 consists of phosphorylases and hydrolases for beta-mannosides. Here, we characterized beta-1,2-mannobiose phosphorylase from Listeria innocua (Lin0857) and determined its crystal structures complexed with beta-1,2-linked mannooligosaccharides. beta-1,2-Mannotriose was bound in a U-shape, interacting with a phosphate analog at both ends. Lin0857 has a unique dimer structure connected by a loop, and a significant open-close loop displacement was observed for substrate entry. A long loop, which is exclusively present in Lin0857, covers the active site to limit the pocket size. A structural basis for substrate recognition and phosphorolysis was provided.
Characterization and crystal structure determination of beta-1,2-mannobiose phosphorylase from Listeria innocua.,Tsuda T, Nihira T, Chiku K, Suzuki E, Arakawa T, Nishimoto M, Kitaoka M, Nakai H, Fushinobu S FEBS Lett. 2015 Dec 21;589(24 Pt B):3816-21. doi: 10.1016/j.febslet.2015.11.034. , Epub 2015 Nov 26. PMID:26632508[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tsuda T, Nihira T, Chiku K, Suzuki E, Arakawa T, Nishimoto M, Kitaoka M, Nakai H, Fushinobu S. Characterization and crystal structure determination of beta-1,2-mannobiose phosphorylase from Listeria innocua. FEBS Lett. 2015 Dec 21;589(24 Pt B):3816-21. doi: 10.1016/j.febslet.2015.11.034. , Epub 2015 Nov 26. PMID:26632508 doi:http://dx.doi.org/10.1016/j.febslet.2015.11.034
- ↑ Tsuda T, Nihira T, Chiku K, Suzuki E, Arakawa T, Nishimoto M, Kitaoka M, Nakai H, Fushinobu S. Characterization and crystal structure determination of beta-1,2-mannobiose phosphorylase from Listeria innocua. FEBS Lett. 2015 Dec 21;589(24 Pt B):3816-21. doi: 10.1016/j.febslet.2015.11.034. , Epub 2015 Nov 26. PMID:26632508 doi:http://dx.doi.org/10.1016/j.febslet.2015.11.034
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