4kmi: Difference between revisions
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The | ==Crystal structure of 4-O-beta-D-mannosyl-D-glucose phosphorylase MGP complexed with PO4== | ||
<StructureSection load='4kmi' size='340' side='right'caption='[[4kmi]], [[Resolution|resolution]] 1.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4kmi]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacteroides_fragilis_NCTC_9343 Bacteroides fragilis NCTC 9343]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KMI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KMI FirstGlance]. <br> | |||
</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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=4kmi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kmi OCA], [https://pdbe.org/4kmi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kmi RCSB], [https://www.ebi.ac.uk/pdbsum/4kmi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kmi ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://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> | |||
<div class="pdbe-citations 4kmi" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bacteroides fragilis NCTC 9343]] | |||
[[Category: Large Structures]] | |||
[[Category: Higa M]] | |||
[[Category: Hijikata A]] | |||
[[Category: Ito S]] | |||
[[Category: Nakae S]] | |||
[[Category: Senoura T]] | |||
[[Category: Shionyu M]] | |||
[[Category: Shirai T]] | |||
[[Category: Wasaki J]] | |||
Latest revision as of 14:30, 8 November 2023
Crystal structure of 4-O-beta-D-mannosyl-D-glucose phosphorylase MGP complexed with PO4
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