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| | {{STRUCTURE_1lvh| PDB=1lvh | SCENE= }} | | {{STRUCTURE_1lvh| PDB=1lvh | SCENE= }} |
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| - | '''The Structure of Phosphorylated beta-phosphoglucomutase from Lactoccocus lactis to 2.3 angstrom resolution'''
| + | ===The Structure of Phosphorylated beta-phosphoglucomutase from Lactoccocus lactis to 2.3 angstrom resolution=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_12081483}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 12081483 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_12081483}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Had superfamily]] | | [[Category: Had superfamily]] |
| | [[Category: Phosphoaspartate]] | | [[Category: Phosphoaspartate]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:20:11 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 22:26:07 2008'' |
Revision as of 19:26, 2 July 2008
Template:STRUCTURE 1lvh
The Structure of Phosphorylated beta-phosphoglucomutase from Lactoccocus lactis to 2.3 angstrom resolution
Template:ABSTRACT PUBMED 12081483
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
Page seeded by OCA on Wed Jul 2 22:26:07 2008
