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Moth chemosensory protein exhibits drastic conformational changes and cooperativity on ligand binding.

Abstract：

:Chemosensory proteins (CSPs) have been proposed to transport hydrophobic chemicals from air to olfactory or taste receptors. They have been isolated from several sensory organs of a wide range of insect species. The x-ray structure of CSPMbraA6, a 112-aa antennal protein from the moth Mamestra brassicae (Mbra), was shown to exhibit a novel type of alpha-helical fold. We have performed a structural and binding study of CSPMbraA6 to get some insights into its possible molecular function. Tryptophan fluorescence quenching demonstrates the ability of CSPMbraA6 to bind several types of semio-chemicals or surrogate ligands with microM K(d). Its crystal structure in complex with one of these compounds, 12-bromo-dodecanol, reveals extensive conformational changes on binding, resulting in the formation of a large cavity filled by three ligand molecules. Furthermore, binding cooperativity was demonstrated for some ligands, suggesting a stepwise binding. The peculiar rearrangement of CSPMbraA6 conformation and the cooperativity phenomenon might trigger the recognition of chemicals by receptors and induce subsequent signal transduction.

journal_name

Proc Natl Acad Sci U S A

journal_title

Proceedings of the National Academy of Sciences of the United States of America

authors

Campanacci V,Lartigue A,Hällberg BM,Jones TA,Giudici-Orticoni MT,Tegoni M,Cambillau C

doi

10.1073/pnas.0836654100

keywords:

subject

Has Abstract

pub_date

2003-04-29 00:00:00

pages

5069-74

issue

9

eissn

0027-8424

issn

1091-6490

pii

0836654100

journal_volume

100

pub_type

杂志文章

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