SBBq
XL Annual Meeting of Brazilian Biochemistry and Molecular Biology Society
th
rd
Foz do Iguaçu, PR, Brazil, April 30 to May 3 , 2011
Crystal Structure of a PIII Metaloproteinase from the Venom of Bothrops moojeni
A. Ullah1,2, Priscila G. Oliveira3, M. T. Murakami3, F. P. de Souza1,2, C. Betzel4; R. K.
Arni1,2
Centro Multiusuário de Inovação Biomolecular e 2Departamento de Física, UNESP,
SJRP-SP, 3Laboratório Nacional de Biociências, Centro Nacional de Pesquisa em
Energia e Materiais, Campinas; 4Laboratory of Structural Biology of Infection and
Inflammation, Hamburg.
1
Snake venom metalloproteinases (SVMPs) and ADAMs (a disintegrin and
metalloproteinase) belong to the Reprolysin family of metalloproteinases. The P III
SVMPs enzymes are especially interesting since they contain proteinase, disintegrin-like
and cystine-rich domains and result in more potent hemorrhage than either the PI or PII
enzymes. Whereas the proteinase domain is implicated in the degradation of capillary
basement membranes and endothelial cell surfaces, the cysteine rich /disintegrin-like
domains are potent inhibitors of collagen induced platelet aggregation and also
modulate the interaction with von Willebrand factor. In order to understand the multiple
roles played by the domains of PIII SVMPs we purified, characterized, crystallized and
determined the structure of the PIII metalloproteinase from the venom of Bothrops
moojeni. The crystals belong to the space group I4(1)22 with cell constants of a
=108.16, b =108.16, c = 196.09 Å, contain one molecule in the asymmetric unit and the
structure was determined and refined at 3.3 Å. Structural comparisons with other PIII
enzymes indicate that the domains adopt different conformations and indicate their
mode of action.
Keywords: metaloproteinase, disintegrin, cystine-rich domain, crystal structure.
Acknowledgements: Supported by CNPq, FAPESP, CAPES, DAAD, TWAS.
���������������������������������������������������������������������������
���������������������������������������������������������������������������������
�����������������������������������������������������