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Crystallization and preliminary X-ray diffraction analysis of a novel Arg49 phospholipase A2 homologue from Zhaoermia mangshanensis venom.

ABSTRACT: Zhaoermiatoxin, an Arg49 phospholipase A2 homologue from Zhaoermia mangshanensis (formerly Trimeresurus mangshanensis, Ermia mangshanensis) venom is a novel member of the PLA2-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 PLA2 homologues, zhaoermiatoxin induces oedema and strong myonecrosis without detectable PLA2 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 A 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 A.

SUBMITTER: Murakami MT

PROVIDER: S-EPMC2335147 | biostudies-literature | 2007 Jul

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray diffraction analysis of a novel Arg49 phospholipase A2 homologue from Zhaoermia mangshanensis venom.

Murakami Mário T MT Kuch Ulrich U Mebs Dietrich D Arni Raghuvir K RK

Acta crystallographica. Section F, Structural biology and crystallization communications 20070622 Pt 7

Zhaoermiatoxin, an Arg49 phospholipase A2 homologue from Zhaoermia mangshanensis (formerly Trimeresurus mangshanensis, Ermia mangshanensis) venom is a novel member of the PLA2-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 PLA2 homologues, zhaoermiatoxin induces oedema and strong myonecrosis without detectable PLA2 catalytic activity ...[more]

PMID: 17620723

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