4bnd
From Proteopedia
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| - | + | ==Structure of an atypical alpha-phosphoglucomutase similar to eukaryotic phosphomannomutases== | |
| - | + | <StructureSection load='4bnd' size='340' side='right' caption='[[4bnd]], [[Resolution|resolution]] 1.50Å' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[4bnd]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lactococcus_lactis_subsp._cremoris_mg1363 Lactococcus lactis subsp. cremoris mg1363]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BND OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BND FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoglucomutase Phosphoglucomutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.2 5.4.2.2] </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=4bnd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bnd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4bnd RCSB], [http://www.ebi.ac.uk/pdbsum/4bnd PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The first structure of a bacterial alpha-phosphoglucomutase with an overall fold similar to eukaryotic phosphomannomutases is reported. Unlike most alpha-phosphoglucomutases within the alpha-D-phosphohexomutase superfamily, it belongs to subclass IIb of the haloacid dehalogenase superfamily (HADSF). It catalyzes the reversible conversion of alpha-glucose 1-phosphate to glucose 6-phosphate. The crystal structure of alpha-phosphoglucomutase from Lactococcus lactis (APGM) was determined at 1.5 A resolution and contains a sulfate and a glycerol bound at the enzyme active site that partially mimic the substrate. A dimeric form of APGM is present in the crystal and in solution, an arrangement that may be functionally relevant. The catalytic mechanism of APGM and its strict specificity towards alpha-glucose 1-phosphate are discussed. | ||
| - | + | High-resolution structure of an atypical alpha-phosphoglucomutase related to eukaryotic phosphomannomutases.,Nogly P, Matias PM, de Rosa M, Castro R, Santos H, Neves AR, Archer M Acta Crystallogr D Biol Crystallogr. 2013 Oct 1;69(Pt 10):2008-2016. Epub 2013, Sep 20. PMID:24100319<ref>PMID:24100319</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Lactococcus lactis subsp. cremoris mg1363]] | [[Category: Lactococcus lactis subsp. cremoris mg1363]] | ||
[[Category: Phosphoglucomutase]] | [[Category: Phosphoglucomutase]] | ||
| - | [[Category: Archer, M | + | [[Category: Archer, M]] |
| - | [[Category: Castro, R | + | [[Category: Castro, R]] |
| - | [[Category: Matias, P M | + | [[Category: Matias, P M]] |
| - | [[Category: Neves, A R | + | [[Category: Neves, A R]] |
| - | [[Category: Nogly, P | + | [[Category: Nogly, P]] |
| - | [[Category: Rosa, M De | + | [[Category: Rosa, M De]] |
| - | [[Category: Santos, H | + | [[Category: Santos, H]] |
[[Category: Isomerase]] | [[Category: Isomerase]] | ||
[[Category: Phosphoglucose interconversion]] | [[Category: Phosphoglucose interconversion]] | ||
[[Category: Substrate specificity]] | [[Category: Substrate specificity]] | ||
Revision as of 12:32, 4 January 2015
Structure of an atypical alpha-phosphoglucomutase similar to eukaryotic phosphomannomutases
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