This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

4kmi

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 23:17, 4 August 2016

Crystal structure of 4-O-beta-D-mannosyl-D-glucose phosphorylase MGP complexed with PO4

Structural highlights

4kmi 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:	3was, 3wat, 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/4kmi"

@@ Line 1: / Line 1: @@
 ==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]] 1.80&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=4kmi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kmi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4kmi RCSB], [http://www.ebi.ac.uk/pdbsum/4kmi 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=4kmi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kmi OCA], [http://pdbe.org/4kmi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4kmi RCSB], [http://www.ebi.ac.uk/pdbsum/4kmi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4kmi 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 4kmi" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

4kmi

From Proteopedia

Revision as of 23:17, 4 August 2016

Crystal structure of 4-O-beta-D-mannosyl-D-glucose phosphorylase MGP complexed with PO4

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox