5b0r

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==Beta-1,2-Mannobiose phosphorylase from Listeria innocua - beta-1,2-mannobiose complex==
==Beta-1,2-Mannobiose phosphorylase from Listeria innocua - beta-1,2-mannobiose complex==
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<StructureSection load='5b0r' size='340' side='right' caption='[[5b0r]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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<StructureSection load='5b0r' size='340' side='right'caption='[[5b0r]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5b0r]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5B0R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5B0R FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5b0r]] 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=5B0R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5B0R FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <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>
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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]] 1.8&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5b0p|5b0p]], [[5b0q|5b0q]], [[5b0s|5b0s]]</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=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <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>
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<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=5b0r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b0r OCA], [http://pdbe.org/5b0r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5b0r RCSB], [http://www.ebi.ac.uk/pdbsum/5b0r PDBsum]</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=5b0r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b0r OCA], [https://pdbe.org/5b0r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5b0r RCSB], [https://www.ebi.ac.uk/pdbsum/5b0r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5b0r ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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<ref>PMID:26632508</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 5b0r" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Arakawa, T]]
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[[Category: Large Structures]]
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[[Category: Fushinobu, S]]
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[[Category: Listeria innocua Clip11262]]
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[[Category: Tsuda, T]]
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[[Category: Arakawa T]]
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[[Category: Glycoside phosphorylase]]
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[[Category: Fushinobu S]]
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[[Category: Transferase]]
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[[Category: Tsuda T]]

Current revision

Beta-1,2-Mannobiose phosphorylase from Listeria innocua - beta-1,2-mannobiose complex

PDB ID 5b0r

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