2dso | pdb_00002dso

Crystal structure of D138N mutant of Drp35, a 35kDa drug responsive protein from Staphylococcus aureus

spinqualitylabelsall models 2dso, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2dso is a 6 chain structure with sequence from "micrococcus_aureus"_(rosenbach_1884)_zopf_1885 "micrococcus aureus" (rosenbach 1884) zopf 1885. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA, GOL Related: 2dg0, 2dg1 Activity: 1,4-lactonase, with EC number 3.1.1.25 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [DRP35_STAAM] Exhibits lactonase activity. Acts in cells with perturbed membrane integrity and is possibly related to the membrane homeostasis (By similarity). 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 Drp35 is a protein induced by cell wall-affecting antibiotics or detergents; it possesses calcium-dependent lactonase activity. To determine the molecular basis of the lactonase activity, we first solved the crystal structures of Drp35 with and without Ca(2+); these showed that the molecule has a six-bladed beta-propeller structure with two calcium ions bound at the center of the beta-propeller and surface region. Mutational analyses of evolutionarily conserved residues revealed that the central calcium-binding site is essential for the enzymatic activity of Drp35. Substitution of some other amino acid residues for the calcium-binding residues demonstrated the critical contributions of Glu(48), Asp(138), and Asp(236) to the enzymatic activity. Differential scanning calorimetric analysis revealed that the loss of activity of E48Q and D236N, but not D138N, was attributed to their inability to hold the calcium ion. Further structural analysis of the D138N mutant indicates that it lacks a water molecule bound to the calcium ion rather than the calcium ion itself. Based on these observations and structural information, a possible catalytic mechanism in which the calcium ion and its binding residues play direct roles was proposed for the lactonase activity of Drp35. Structural and mutational analyses of Drp35 from Staphylococcus aureus: a possible mechanism for its lactonase activity.,Tanaka Y, Morikawa K, Ohki Y, Yao M, Tsumoto K, Watanabe N, Ohta T, Tanaka I J Biol Chem. 2007 Feb 23;282(8):5770-80. Epub 2006 Dec 13. PMID:17166853 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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