1lvh: Difference between revisions
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[[Image:1lvh.gif|left|200px]] | [[Image:1lvh.gif|left|200px]] | ||
'''The Structure of Phosphorylated beta-phosphoglucomutase from Lactoccocus lactis to 2.3 angstrom resolution''' | {{Structure | ||
|PDB= 1lvh |SIZE=350|CAPTION= <scene name='initialview01'>1lvh</scene>, resolution 2.30Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene> | |||
|ACTIVITY= [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] | |||
|GENE= PGMB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1358 Lactococcus lactis]) | |||
}} | |||
'''The Structure of Phosphorylated beta-phosphoglucomutase from Lactoccocus lactis to 2.3 angstrom resolution''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1LVH is a [ | 1LVH is a [[Single protein]] structure of 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=1LVH OCA]. | ||
==Reference== | ==Reference== | ||
Caught in the act: the structure of phosphorylated beta-phosphoglucomutase from Lactococcus lactis., Lahiri SD, Zhang G, Dunaway-Mariano D, Allen KN, Biochemistry. 2002 Jul 2;41(26):8351-9. PMID:[http:// | Caught in the act: the structure of phosphorylated beta-phosphoglucomutase from Lactococcus lactis., Lahiri SD, Zhang G, Dunaway-Mariano D, Allen KN, Biochemistry. 2002 Jul 2;41(26):8351-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12081483 12081483] | ||
[[Category: Beta-phosphoglucomutase]] | [[Category: Beta-phosphoglucomutase]] | ||
[[Category: Lactococcus lactis]] | [[Category: Lactococcus lactis]] | ||
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[[Category: phosphoaspartate]] | [[Category: phosphoaspartate]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:35:44 2008'' | ||
Revision as of 13:35, 20 March 2008
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| , resolution 2.30Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | PGMB (Lactococcus lactis) | ||||||
| Activity: | Beta-phosphoglucomutase, with EC number 5.4.2.6 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
The Structure of Phosphorylated beta-phosphoglucomutase from Lactoccocus lactis to 2.3 angstrom resolution
OverviewOverview
Phosphoglucomutases catalyze the interconversion of D-glucose 1-phosphate and D-glucose 6-phosphate, a reaction central to energy metabolism in all cells and to the synthesis of cell wall polysaccharides in bacterial cells. Two classes of phosphoglucomutases (alpha-PGM and beta-PGM) are distinguished on the basis of their specificity for alpha- and beta-glucose-1-phosphate. beta-PGM is a member of the haloacid dehalogenase (HAD) superfamily, which includes the sarcoplasmic Ca(2+)-ATPase, phosphomannomutase, and phosphoserine phosphatase. beta-PGM is unusual among family members in that the common phosphoenzyme intermediate exists as a stable ground-state complex in this enzyme. Herein we report, for the first time, the three-dimensional structure of a beta-PGM and the first view of the true phosphoenzyme intermediate in the HAD superfamily. The crystal structure of the Mg(II) complex of phosphorylated beta-phosphoglucomutase (beta-PGM) from Lactococcus lactis has been determined to 2.3 A resolution by multiwavelength anomalous diffraction (MAD) phasing on selenomethionine, and refined to an R(cryst) = 0.24 and R(free) = 0.28. The active site of beta-PGM is located between the core and the cap domain and is freely solvent accessible. The residues within a 6 A radius of the phosphorylated Asp8 include Asp10, Thr16, Ser114, Lys145, Glu169, and Asp170. The cofactor Mg(2+) is liganded with octahedral coordination geometry by the carboxylate side chains of Asp8, Glu169, Asp170, and the backbone carbonyl oxygen of Asp10 along with one oxygen from the Asp8-phosphoryl group and one water ligand. The phosphate group of the phosphoaspartyl residue, Asp8, interacts with the side chains of Ser114 and Lys145. The absence of a base residue near the aspartyl phosphate group accounts for the persistence of the phosphorylated enzyme under physiological conditions. Substrate docking shows that glucose-6-P can bind to the active site of phosphorylated beta-PGM in such a way as to position the C(1)OH near the phosphoryl group of the phosphorylated Asp8 and the C(6) phosphoryl group near the carboxylate group of Asp10. This result suggests a novel two-base mechanism for phosphoryl group transfer in a phosphorylated sugar.
About this StructureAbout this Structure
1LVH is a Single protein structure of sequence from Lactococcus lactis. Full crystallographic information is available from OCA.
ReferenceReference
Caught in the act: the structure of phosphorylated beta-phosphoglucomutase from Lactococcus lactis., Lahiri SD, Zhang G, Dunaway-Mariano D, Allen KN, Biochemistry. 2002 Jul 2;41(26):8351-9. PMID:12081483
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