5ok1: Difference between revisions

Revision as of 10:15, 29 August 2018

D10N variant of beta-phosphoglucomutase from Lactococcus lactis trapped with native beta-glucose 1,6-bisphosphate intermediate to 1.9A resolution.D10N variant of beta-phosphoglucomutase from Lactococcus lactis trapped with native beta-glucose 1,6-bisphosphate intermediate to 1.9A resolution.

Structural highlights

5ok1 is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Activity:	Beta-phosphoglucomutase, with EC number 5.4.2.6
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.^[1] ^[2]

References

↑ Qian N, Stanley GA, Bunte A, Radstrom P. Product formation and phosphoglucomutase activities in Lactococcus lactis: cloning and characterization of a novel phosphoglucomutase gene. Microbiology. 1997 Mar;143 ( Pt 3):855-65. PMID:9084169
↑ Lahiri SD, Zhang G, Dai J, Dunaway-Mariano D, Allen KN. Analysis of the substrate specificity loop of the HAD superfamily cap domain. Biochemistry. 2004 Mar 16;43(10):2812-20. PMID:15005616 doi:10.1021/bi0356810

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OCA

[1] Qian N, Stanley GA, Bunte A, Radstrom P. Product formation and phosphoglucomutase activities in Lactococcus lactis: cloning and characterization of a novel phosphoglucomutase gene. Microbiology. 1997 Mar;143 ( Pt 3):855-65. PMID:9084169

[2] Lahiri SD, Zhang G, Dai J, Dunaway-Mariano D, Allen KN. Analysis of the substrate specificity loop of the HAD superfamily cap domain. Biochemistry. 2004 Mar 16;43(10):2812-20. PMID:15005616 doi:10.1021/bi0356810

[1]

[2]

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5ok1 is ON HOLD  until Paper Publication
+==D10N variant of beta-phosphoglucomutase from Lactococcus lactis trapped with native beta-glucose 1,6-bisphosphate intermediate to 1.9A resolution.==
+<StructureSection load='5ok1' size='340' side='right' caption='[[5ok1]], [[Resolution|resolution]] 1.86&Aring;' scene=''>
-Authors:
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5ok1]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OK1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5OK1 FirstGlance]. <br>
-Description:
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=B16:1,6-DI-O-PHOSPHONO-BETA-D-GLUCOPYRANOSE'>B16</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-[[Category: Unreleased Structures]]
+<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>
+<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=5ok1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ok1 OCA], [http://pdbe.org/5ok1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ok1 RCSB], [http://www.ebi.ac.uk/pdbsum/5ok1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ok1 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[[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>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Beta-phosphoglucomutase]]
+[[Category: Bisson, C]]
+[[Category: Robertson, A J]]
+[[Category: Bisphospho-intermediate]]
+[[Category: Isomerase]]
+[[Category: Phosphoglucomutase]]

5ok1: Difference between revisions

Revision as of 10:15, 29 August 2018

D10N variant of beta-phosphoglucomutase from Lactococcus lactis trapped with native beta-glucose 1,6-bisphosphate intermediate to 1.9A resolution.D10N variant of beta-phosphoglucomutase from Lactococcus lactis trapped with native beta-glucose 1,6-bisphosphate intermediate to 1.9A resolution.

Structural highlights

Function

References

Contents

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5ok1: Difference between revisions

Revision as of 10:15, 29 August 2018

D10N variant of beta-phosphoglucomutase from Lactococcus lactis trapped with native beta-glucose 1,6-bisphosphate intermediate to 1.9A resolution.D10N variant of beta-phosphoglucomutase from Lactococcus lactis trapped with native beta-glucose 1,6-bisphosphate intermediate to 1.9A resolution.

Structural highlights

Function

References

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