3uwd | pdb_00003uwd

Crystal Structure of Phosphoglycerate Kinase from Bacillus Anthracis

spinqualitylabelsall models 3uwd, resolution 1.68Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3uwd is a 1 chain structure with sequence from Bacillus anthracis. This structure supersedes the now removed PDB entry 3b2b. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BTB, CL, MG, UNL NonStd Res: MSE Gene: BAS4988, BA_5367, GBAA_5367, pgk (Bacillus anthracis) Activity: Phosphoglycerate kinase, with EC number 2.7.2.3 Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed Phosphoglycerate kinase (PGK) is indispensable during glycolysis for anaerobic glucose degradation and energy generation. Here we present comprehensive structure analysis of two putative PGKs from Bacillus anthracis str. Sterne and Campylobacter jejuni in the context of their structural homologs. They are the first PGKs from pathogenic bacteria reported in the Protein Data Bank. The crystal structure of PGK from Bacillus anthracis str. Sterne (BaPGK) has been determined at 1.68 A while the structure of PGK from Campylobacter jejuni (CjPGK) has been determined at 2.14 A resolution. The proteins' monomers are composed of two domains, each containing a Rossmann fold, hinged together by a helix which can be used to adjust the relative position between two domains. It is also shown that apo-forms of both BaPGK and CjPGK adopt open conformations as compared to the substrate and ATP bound forms of PGK from other species. Crystal structures of putative phosphoglycerate kinases from B. anthracis and C. jejuni.,Zheng H, Filippova EV, Tkaczuk KL, Dworzynski P, Chruszcz M, Porebski PJ, Wawrzak Z, Onopriyenko O, Kudritska M, Grimshaw S, Savchenko A, Anderson WF, Minor W J Struct Funct Genomics. 2012 Mar;13(1):15-26. Epub 2012 Mar 10. PMID:22403005 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Phosphoglycerate Kinase

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