2x98 | pdb_00002x98

H.SALINARUM ALKALINE PHOSPHATASE

spinqualitylabelsall models 2x98, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2x98 is a 2 chain structure with sequence from Halobacterium salinarum R1. This structure supersedes the now removed PDB entry 2w0y. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.7Å Ligands: CL, MG, NA, PO4, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function B0R9W3_HALS3 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 Phosphate is an essential component of all cells that must be taken up from the environment. Prokaryotes commonly secrete alkaline phosphatases (APs) to recruit phosphate from organic compounds by hydrolysis. In this study, the AP from Halobacterium salinarum, an archaeon that lives in a saturated salt environment, has been functionally and structurally characterized. The core fold and the active-site architecture of the H. salinarum enzyme are similar to other AP structures. These generally form dimers composed of dominant beta-sheet structures sandwiched by alpha-helices and have well-accessible active sites. The surface of the enzyme is predicted to be highly negatively charged, like other proteins of extreme halophiles. In addition to the conserved core, most APs contain a crown domain that strongly varies within species. In the H. salinarum AP, the crown domain is made of an acyl-carrier-protein-like fold. Different from other APs, it is not involved in dimer formation. We compare the archaeal AP with its bacterial and eukaryotic counterparts, and we focus on the role of crown domains in enhancing protein stability, regulating enzyme function, and guiding phosphoesters into the active-site funnel. Structural and biochemical characterization of a halophilic archaeal alkaline phosphatase.,Wende A, Johansson P, Vollrath R, Dyall-Smith M, Oesterhelt D, Grininger M J Mol Biol. 2010 Jul 2;400(1):52-62. Epub 2010 May 11. PMID:20438737 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Alkaline phosphatase 3D structures

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