3ipr | pdb_00003ipr

Crystal structure of the Enterococcus faecalis gluconate specific EIIA phosphotransferase system component

spinqualitylabelsall models 3ipr, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3ipr is a 6 chain structure with sequence from "enterococcus_proteiformis"_thiercelin_and_jouhaud_1903 "enterococcus proteiformis" thiercelin and jouhaud 1903. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA Gene: EF_3136, gntF ("Enterococcus proteiformis" Thiercelin and Jouhaud 1903) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 In Eubacteria, the utilization of a number of extracellular carbohydrates is mediated by sugar specific phosphoenolepyruvate (PEP) dependent sugar phosphotransferase systems (PTSs), which simultaneously import und phosphorylate their target sugars. Here, we report the crystal structure of the EIIA(gnt) component of the so far little investigated Enterococcus faecalis gluconate specific PTS. The crystal structure shows a tightly interacting dimer of EIIA(gnt) which is structurally similar to the related EIIA(man) from Escherichia coli. Homology modeling of E. faecalis HPr, EIIB(man) and their complexes with EIIA(man) suggests that despite moderate sequence identity between EIIA(man) and EIIA(gnt), the active sites closely match the situation observed in the E. coli system with His-9 of EIIA(gnt) being the likely phosphoryl group carrier. We therefore propose that the phosphoryl transfer reactions involving EIIA(gnt) proceed according to a mechanism analog to the one described for E. coli EIIA(man). Structure of the Enterococcus faecalis EIIA(gnt) PTS component.,Reinelt S, Koch B, Hothorn M, Hengstenberg W, Welti S, Scheffzek K Biochem Biophys Res Commun. 2009 Oct 30;388(4):626-9. Epub 2009 Aug 13. PMID:19682976 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Phosphotransferase

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