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3wat

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Revision as of 18:15, 4 August 2016

Crystal structure of 4-O-beta-D-mannosyl-D-glucose phosphorylase MGP complexed with Man+Glc

Structural highlights

3wat is a 2 chain structure with sequence from Bacfn. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Related:	4kmi, 3was, 3wau
Gene:	BF0772 (BACFN)
Activity:	4-O-beta-D-mannosyl-D-glucose phosphorylase, with EC number 2.4.1.281
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.^[1]

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^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Senoura T, Ito S, Taguchi H, Higa M, Hamada S, Matsui H, Ozawa T, Jin S, Watanabe J, Wasaki J, Ito S. New microbial mannan catabolic pathway that involves a novel mannosylglucose phosphorylase. Biochem Biophys Res Commun. 2011 May 20;408(4):701-6. doi:, 10.1016/j.bbrc.2011.04.095. Epub 2011 Apr 24. PMID:21539815 doi:10.1016/j.bbrc.2011.04.095
↑ Nakae S, Ito S, Higa M, Senoura T, Wasaki J, Hijikata A, Shionyu M, Ito S, Shirai T. Structure of Novel Enzyme in Mannan Biodegradation Process 4-O-beta-d-Mannosyl-d-Glucose Phosphorylase MGP. J Mol Biol. 2013 Aug 14. pii: S0022-2836(13)00505-6. doi:, 10.1016/j.jmb.2013.08.002. PMID:23954514 doi:10.1016/j.jmb.2013.08.002

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3wat"

@@ Line 1: / Line 1: @@
 ==Crystal structure of 4-O-beta-D-mannosyl-D-glucose phosphorylase MGP complexed with Man+Glc==
 <StructureSection load='3wat' size='340' side='right' caption='[[3wat]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
@@ Line 7: / Line 8: @@
 <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=3wat FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wat OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wat RCSB], [http://www.ebi.ac.uk/pdbsum/3wat PDBsum]</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=3wat FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wat OCA], [http://pdbe.org/3wat PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3wat RCSB], [http://www.ebi.ac.uk/pdbsum/3wat PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3wat ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 19: / Line 20: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 3wat" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

3wat

From Proteopedia

Revision as of 18:15, 4 August 2016

Crystal structure of 4-O-beta-D-mannosyl-D-glucose phosphorylase MGP complexed with Man+Glc

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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