3rlg

Crystal structure of Loxosceles intermedia phospholipase D isoform 1 H12A mutant

spinqualitylabelsall models 3rlg, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3rlg is a 1 chain structure with sequence from Brown spider. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: EDO, MG, PEG, PGE Related: 3rlh Activity: Sphingomyelin phosphodiesterase D, with EC number 3.1.4.41 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [A1HA_LOXIN] Catalyzes the hydrolysis of sphingomyelin, lysophosphatidylcholine, and lyso-platelet activating factor but not that of phosphatidylcholine. Shows a high enzymatic activity. Induces dermonecrosis, blood vessel permeability and platelet aggregation (PubMed:9790962). Is directly toxic to kidney (PubMed:16005484) and liver (PubMed:18765244). Also induces hemolysis in a complement-dependent manner (PubMed:9790962) as well as in a complement-independent manner. The hemolysis provoked in a complement-independent manner is composed of several steps. The toxin binds to erythrocyte membranes, hydrolyzes membrane phospholipids (sphingomyelin and lysophosphatidylcholine) thus generating metabolism products that cause hemolysis, probably by provoking an increase of calcium inside cells. The calcium influx is due to the opening of L-type calcium channels, since L-type calcium channel blockers inhibit calcium influx (PubMed:21590705). Publication Abstract from PubMed Phospholipases D are the major dermonecrotic component of Loxosceles venom and catalyze the hydrolysis of phospholipids, resulting in the formation of lipid mediators such as ceramide-1-phosphate and lysophosphatidic acid which can induce pathological and biological responses. Phospholipases D can be classified into two classes depending on their catalytic efficiency and the presence of an additional disulfide bridge. In this work, both wild-type and H12A-mutant forms of the class II phospholipase D from L. intermedia venom were crystallized. Wild-type and H12A-mutant crystals were grown under very similar conditions using PEG 200 as a precipitant and belonged to space group P12(1)1, with unit-cell parameters a = 50.1, b = 49.5, c = 56.5 A, beta = 105.9 degrees . Wild-type and H12A-mutant crystals diffracted to maximum resolutions of 1.95 and 1.60 A, respectively. Crystallization and preliminary X-ray diffraction analysis of a class II phospholipase D from Loxosceles intermedia venom.,Ullah A, de Giuseppe PO, Murakami MT, Trevisan-Silva D, Wille AC, Chaves-Moreira D, Gremski LH, da Silveira RB, Sennf-Ribeiro A, Chaim OM, Veiga SS, Arni RK Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Feb 1;67(Pt, 2):234-6. Epub 2011 Jan 22. PMID:21301094 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Phospholipase D Sphingomyelinase

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