3wau
From Proteopedia
(Difference between revisions)
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| - | + | ==Crystal structure of 4-O-beta-D-mannosyl-D-glucose phosphorylase MGP complexed with M1P== | |
| - | + | <StructureSection load='3wau' size='340' side='right' caption='[[3wau]], [[Resolution|resolution]] 1.70Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[3wau]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacfn Bacfn]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WAU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WAU FirstGlance]. <br> | |
| - | ==Function== | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=M1P:ALPHA-D-MANNOSE+1-PHOSPHATE'>M1P</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4kmi|4kmi]], [[3was|3was]], [[3wat|3wat]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BF0772 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272559 BACFN])</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/4-O-beta-D-mannosyl-D-glucose_phosphorylase 4-O-beta-D-mannosyl-D-glucose phosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.281 2.4.1.281] </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=3wau FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wau OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wau RCSB], [http://www.ebi.ac.uk/pdbsum/3wau PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
[[http://www.uniprot.org/uniprot/MGP_BACFN MGP_BACFN]] Converts 4-O-beta-D-mannopyranosyl-D-glucopyranose (Man-Glc) to mannose 1-phosphate (Man1P) and glucose. Involved in a mannan catabolic pathway which feeds into glycolysis.<ref>PMID:21539815</ref> | [[http://www.uniprot.org/uniprot/MGP_BACFN MGP_BACFN]] Converts 4-O-beta-D-mannopyranosyl-D-glucopyranose (Man-Glc) to mannose 1-phosphate (Man1P) and glucose. Involved in a mannan catabolic pathway which feeds into glycolysis.<ref>PMID:21539815</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The crystal structure of a novel component of the mannan biodegradation system, 4-O-beta-d-mannosyl-d-glucose phosphorylase (MGP), was determined to a 1.68-A resolution. The structure of the enzyme revealed a unique homohexameric structure, which was formed by using two helices attached to the N-terminus and C-terminus as a tab for sticking between subunits. The structures of MGP complexes with genuine substrates, 4-O-beta-d-mannosyl-d-glucose and phosphate, and the product d-mannose-1-phosphate were also determined. The complex structures revealed that the invariant residue Asp131, which is supposed to be the general acid/base, did not exist close to the glycosidic Glc-O4 atom, which should be protonated in the catalytic reaction. Also, no solvent molecule that might mediate a proton transfer from Asp131 was observed in the substrate complex structure, suggesting that the catalytic mechanism of MGP is different from those of known disaccharide phosphorylases. | ||
| - | + | Structure of Novel Enzyme in Mannan Biodegradation Process 4-O-beta-d-Mannosyl-d-Glucose Phosphorylase MGP.,Nakae S, Ito S, Higa M, Senoura T, Wasaki J, Hijikata A, Shionyu M, Ito S, Shirai T J Mol Biol. 2013 Aug 14. pii: S0022-2836(13)00505-6. doi:, 10.1016/j.jmb.2013.08.002. PMID:23954514<ref>PMID:23954514</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: 4-O-beta-D-mannosyl-D-glucose phosphorylase]] | [[Category: 4-O-beta-D-mannosyl-D-glucose phosphorylase]] | ||
[[Category: Bacfn]] | [[Category: Bacfn]] | ||
| - | [[Category: Higa, M | + | [[Category: Higa, M]] |
| - | [[Category: Hijikata, A | + | [[Category: Hijikata, A]] |
| - | [[Category: Ito, S | + | [[Category: Ito, S]] |
| - | [[Category: Nakae, S | + | [[Category: Nakae, S]] |
| - | [[Category: Senoura, T | + | [[Category: Senoura, T]] |
| - | [[Category: Shionyu, M | + | [[Category: Shionyu, M]] |
| - | [[Category: Shirai, T | + | [[Category: Shirai, T]] |
| - | [[Category: Wasaki, J | + | [[Category: Wasaki, J]] |
[[Category: 5-bladed beta propeller fold]] | [[Category: 5-bladed beta propeller fold]] | ||
[[Category: Mannan biodegradation]] | [[Category: Mannan biodegradation]] | ||
[[Category: Phosphorylase]] | [[Category: Phosphorylase]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
Revision as of 15:21, 25 December 2014
Crystal structure of 4-O-beta-D-mannosyl-D-glucose phosphorylase MGP complexed with M1P
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