2wf9

Structure of Beta-Phosphoglucomutase inhibited with Glucose-6- phosphate, and Beryllium trifluoride, crystal form 2Structure of Beta-Phosphoglucomutase inhibited with Glucose-6- phosphate, and Beryllium trifluoride, crystal form 2

Structural highlights 2wf9 is a 1 chain structure with sequence from "bacterium_lactis"_lister_1873 "bacterium lactis" lister 1873. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: , , , , Related: 1z4o, 1o03, 1zol, 1z4n, 1o08, 1lvh, 2wf5, 2wf6, 2wf7, 2wf8, 2wfa 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. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Experimental observations of fluoromagnesate and fluoroaluminate complexes of beta-phosphoglucomutase (beta-PGM) have demonstrated the importance of charge balance in transition-state stabilization for phosphoryl transfer enzymes. Here, direct observations of ground-state analog complexes of beta-PGM involving trifluoroberyllate establish that when the geometry and charge distribution closely match those of the substrate, the distribution of conformers in solution and in the crystal predominantly places the reacting centers in van der Waals proximity. Importantly, two variants are found, both of which satisfy the criteria for near attack conformers. In one variant, the aspartate general base for the reaction is remote from the nucleophile. The nucleophile remains protonated and forms a nonproductive hydrogen bond to the phosphate surrogate. In the other variant, the general base forms a hydrogen bond to the nucleophile that is now correctly orientated for the chemical transfer step. By contrast, in the absence of substrate, the solvent surrounding the phosphate surrogate is arranged to disfavor nucleophilic attack by water. Taken together, the trifluoroberyllate complexes of beta-PGM provide a picture of how the enzyme is able to organize itself for the chemical step in catalysis through the population of intermediates that respond to increasing proximity of the nucleophile. These experimental observations show how the enzyme is capable of stabilizing the reaction pathway toward the transition state and also of minimizing unproductive catalysis of aspartyl phosphate hydrolysis. Near attack conformers dominate beta-phosphoglucomutase complexes where geometry and charge distribution reflect those of substrate.,Griffin JL, Bowler MW, Baxter NJ, Leigh KN, Dannatt HR, Hounslow AM, Blackburn GM, Webster CE, Cliff MJ, Waltho JP Proc Natl Acad Sci U S A. 2012 May 1;109(18):6910-5. Epub 2012 Apr 13. PMID:22505741 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Beta-phosphoglucomutase 3D structures

spinqualitylabelsall models 2wf9, resolution 1.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image