1o08

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1o08]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lactococcus_lactis Lactococcus lactis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O08 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1O08 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1o08]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lactococcus_lactis Lactococcus lactis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O08 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1O08 FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=G16:ALPHA-D-GLUCOSE+1,6-BISPHOSPHATE'>G16</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene><br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=G16:ALPHA-D-GLUCOSE+1,6-BISPHOSPHATE'>G16</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1lvh|1lvh]]</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1lvh|1lvh]]</td></tr>
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<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-phosphoglucomutase Beta-phosphoglucomutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.6 5.4.2.6] </span></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-phosphoglucomutase Beta-phosphoglucomutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.6 5.4.2.6] </span></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1o08 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o08 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1o08 RCSB], [http://www.ebi.ac.uk/pdbsum/1o08 PDBsum]</span></td></tr>
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<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=1o08 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o08 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1o08 RCSB], [http://www.ebi.ac.uk/pdbsum/1o08 PDBsum]</span></td></tr>
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<table>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/PGMB_LACLA PGMB_LACLA]] Catalyzes the interconversion of D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), forming beta-D-glucose 1,6-(bis)phosphate (beta-G16P) as an intermediate. The beta-phosphoglucomutase (Beta-PGM) acts on the beta-C(1) anomer of G1P. Glucose or lactose are used in preference to maltose, which is only utilized after glucose or lactose has been exhausted. It plays a key role in the regulation of the flow of carbohydrate intermediates in glycolysis and the formation of the sugar nucleotide UDP-glucose.<ref>PMID:9084169</ref> <ref>PMID:15005616</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: Beta-phosphoglucomutase]]
[[Category: Beta-phosphoglucomutase]]
[[Category: Lactococcus lactis]]
[[Category: Lactococcus lactis]]
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[[Category: Allen, K N.]]
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[[Category: Allen, K N]]
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[[Category: Dunaway-Mariano, D.]]
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[[Category: Dunaway-Mariano, D]]
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[[Category: Lahiri, S D.]]
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[[Category: Lahiri, S D]]
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[[Category: Zhang, G.]]
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[[Category: Zhang, G]]
[[Category: Haloacid dehalogenase superfamily]]
[[Category: Haloacid dehalogenase superfamily]]
[[Category: Isomerase]]
[[Category: Isomerase]]
[[Category: Pentavalent phosphate intermediate]]
[[Category: Pentavalent phosphate intermediate]]
[[Category: Phosphotransferase]]
[[Category: Phosphotransferase]]

Revision as of 18:17, 25 December 2014

Structure of Pentavalent Phosphorous Intermediate of an Enzyme Catalyzed Phosphoryl transfer Reaction observed on cocrystallization with Glucose 1-phosphate

1o08, resolution 1.20Å

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