Crystallization and preliminary X-ray diffraction analysis of a novel Arg49 phospholipase A(2) homologue from Zhaoermia mangshanensis venom


Autoria(s): Murakami, Rio T.; Kuch, Ulrich; Mebs, Dietrich; Arni, Raghuvir K.
Contribuinte(s)

Universidade Estadual Paulista (UNESP)

Data(s)

20/05/2014

20/05/2014

01/07/2007

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