Crystallization and preliminary X-ray diffraction analysis of a novel Arg49 phospholipase A(2) homologue from Zhaoermia mangshanensis venom
Contribuinte(s) |
Universidade Estadual Paulista (UNESP) |
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Data(s) |
20/05/2014
20/05/2014
01/07/2007
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Resumo |
Zhaoermiatoxin, an Arg49 phospholipase A(2) homologue from Zhaoermia mangshanensis (formerly Trimeresurus mangshanensis, Ermia mangshanensis) venom is a novel member of the PLA(2)-homologue family that possesses an arginine residue at position 49, probably arising from a secondary Lys49 -> Arg substitution that does not alter the catalytic inactivity towards phospholipids. Like other Lys49 PLA(2) homologues, zhaoermiatoxin induces oedema and strong myonecrosis without detectable PLA(2) catalytic activity. A single crystal with maximum dimensions of 0.2 x 0.2 x 0.5 mm was used for X-ray diffraction data collection to a resolution of 2.05 angstrom using synchrotron radiation and the diffraction pattern was indexed in the hexagonal space group P6(4), with unit-cell parameters a = 72.9, b = 72.9, c = 93.9 angstrom. |
Formato |
605-607 |
Identificador |
http://dx.doi.org/10.1107/S1744309107026073 Acta Crystallographica Section F-structural Biology and Crystallization Communications. Oxford: Blackwell Publishing, v. 63, p. 605-607, 2007. 1744-3091 http://hdl.handle.net/11449/34106 10.1107/S1744309107026073 WOS:000248045300018 |
Idioma(s) |
eng |
Publicador |
Blackwell Publishing |
Relação |
Acta Crystallographica Section F: Structural Biology and Crystallization Communications |
Direitos |
closedAccess |
Tipo |
info:eu-repo/semantics/article |