Journal
STRUCTURE
Volume 19, Issue 1, Pages 26-36Publisher
CELL PRESS
DOI: 10.1016/j.str.2010.11.011
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Funding
- Conselho Nacional de Desenvolvimento Cientifico e Tecnologico (CNPq)
- ICGEB-Trieste
- Fundacao de Amparo a Pesquisa do Estado do Rio de Janeiro Carlos Chagas Filho (FAPERJ-Pensa Rio)
- Coordenacao de Aperfeigoamento de Pessoal de Nivel Superior (CAPES)
- National Institute of Structural Biology and Bioimaging (INBEB)
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Defensins are essentially ancient natural antibiotics with potent activity extending from lower organisms to humans. Sd5 is a recently described antifungal defensin that appears to be the result of a recent gain of function. We reported here the solution NMR structure of Sd5 and characterized the backbone dynamics in the free state and in the presence of membrane models. N-15 relaxation dispersion measurements indicate intrinsic conformational exchange processes, showing two clear distinct k(ex), 490 and 1800 s(-1). These multiple motions may be related to transient twisting or breathing of the alpha helix and beta sheet. The stages of membrane recognition and disruption by Sd5 over a large timescale range were mapped and demonstrated that Sd5 in solution sampled an ensemble of different conformations, of which a subset is selected upon membrane binding. Defensins share similar structures, but we demonstrated here that their dynamics can be extremely diverse.
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