3RLG
Crystal structure of Loxosceles intermedia phospholipase D isoform 1 H12A mutant
Summary for 3RLG
| Entry DOI | 10.2210/pdb3rlg/pdb |
| Related | 3RLH |
| Descriptor | Sphingomyelin phosphodiesterase D LiSicTox-alphaIA1a, MAGNESIUM ION, 1,2-ETHANEDIOL, ... (6 entities in total) |
| Functional Keywords | tim beta/alpha-barrel, plc-like phosphodiesterase, inactive mutant h12a phospholipase d, hydrolase |
| Biological source | Loxosceles intermedia (Spider) |
| Cellular location | Secreted: P0CE80 |
| Total number of polymer chains | 1 |
| Total formula weight | 34457.79 |
| Authors | Giuseppe, P.O.,Ullah, A.,Veiga, S.S.,Murakami, M.T.,Arni, R.K. (deposition date: 2011-04-19, release date: 2011-08-24, Last modification date: 2024-11-20) |
| Primary citation | Ullah, A.,de Giuseppe, P.O.,Murakami, M.T.,Trevisan-Silva, D.,Wille, A.C.,Chaves-Moreira, D.,Gremski, L.H.,da Silveira, R.B.,Sennf-Ribeiro, A.,Chaim, O.M.,Veiga, S.S.,Arni, R.K. Crystallization and preliminary X-ray diffraction analysis of a class II phospholipase D from Loxosceles intermedia venom. Acta Crystallogr.,Sect.F, 67:234-236, 2011 Cited by PubMed Abstract: 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 Å, β = 105.9°. Wild-type and H12A-mutant crystals diffracted to maximum resolutions of 1.95 and 1.60 Å, respectively. PubMed: 21301094DOI: 10.1107/S1744309110050931 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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