1lvh
From Proteopedia
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|PDB= 1lvh |SIZE=350|CAPTION= <scene name='initialview01'>1lvh</scene>, resolution 2.30Å | |PDB= 1lvh |SIZE=350|CAPTION= <scene name='initialview01'>1lvh</scene>, resolution 2.30Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene> | + | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PHD:ASPARTYL+PHOSPHATE'>PHD</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] | + | |ACTIVITY= <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> |
|GENE= PGMB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1358 Lactococcus lactis]) | |GENE= PGMB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1358 Lactococcus lactis]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1fez|1FEZ]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lvh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lvh OCA], [http://www.ebi.ac.uk/pdbsum/1lvh PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1lvh RCSB]</span> | ||
}} | }} | ||
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[[Category: Lahiri, S D.]] | [[Category: Lahiri, S D.]] | ||
[[Category: Zhang, G.]] | [[Category: Zhang, G.]] | ||
| - | [[Category: MG]] | ||
[[Category: aspartylphosphate]] | [[Category: aspartylphosphate]] | ||
[[Category: had superfamily]] | [[Category: had superfamily]] | ||
[[Category: phosphoaspartate]] | [[Category: phosphoaspartate]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:07:56 2008'' |
Revision as of 19:07, 30 March 2008
| |||||||
| , resolution 2.30Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | PGMB (Lactococcus lactis) | ||||||
| Activity: | Beta-phosphoglucomutase, with EC number 5.4.2.6 | ||||||
| Related: | 1FEZ
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
The Structure of Phosphorylated beta-phosphoglucomutase from Lactoccocus lactis to 2.3 angstrom resolution
Overview
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 Structure
1LVH is a Single protein structure of sequence from Lactococcus lactis. Full crystallographic information is available from OCA.
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:12081483
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