Crystallization and preliminary X-ray diffraction analysis of a novel sphingomyelinase D from Loxosceles gaucho venom

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2014-10-01

Autores

Ullah, Anwar [UNESP]
Magalhaes, Geraldo Santana
Masood, Rehana [UNESP]
Mariutti, Ricardo Barros [UNESP]
Coronado, Monika Aparecida [UNESP]
Murakami, Mario Tyago
Barbaro, Katia Cristina
Arni, Raghuvir Krishnaswamy [UNESP]

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Wiley-Blackwell

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Brown spider envenomation results in dermonecrosis, intravascular coagulation, haemolysis and renal failure, mainly owing to the action of sphingomyelinases D (SMases D), which catalyze the hydrolysis of sphingomyelin to produce ceramide 1-phosphate and choline or the hydrolysis of lysophosphatidylcholine to produce lysophosphatidic acid. Here, the heterologous expression, purification, crystallization and preliminary X-ray diffraction analysis of LgRec1, a novel SMase D from Loxosceles gaucho venom, are reported. The crystals belonged to space group P2(1)2(1)2, with unit-cell parameters a = 52.98, b = 62.27, c = 84.84 angstrom and diffracted to a maximum resolution of 2.6 angstrom.

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Acta Crystallographica Section F-structural Biology Communications. Hoboken: Wiley-blackwell, v. 70, p. 1418-1420, 2014.