1k19
From Proteopedia
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NMR Solution Structure of the Chemosensory Protein CSP2 from Moth Mamestra brassicae
Overview
Chemosensory proteins (CSPs) are believed to be involved in chemical, communication and perception. A number of such proteins, of molecular mass, approximately 13 kDa, have been isolated from different sensory organs of, a wide range of insect species. Several CSPs have been identified in the, antennae and proboscis of the moth Mamestra brassicae. CSPMbraA6, a, 112-amino-acid antennal protein, has been expressed in a soluble form in, large quantities in the Escherichi coli periplasm. NMR structure, determination of CSPMbraA6 has been performed with 1H- and 15N-labelled, samples. The calculated structures present an average root mean square, deviation about the mean structure of 0.63 A for backbone atoms and 1.27 A, for all non-hydrogen atoms except the 12 N-terminal residues. The protein, is well folded from residue 12 to residue 110, and consists of a, non-bundle alpha-helical structure with six helices connected by alpha, alpha loops. It has a globular shape, with overall dimensions of 32 A x 28, A x 24 A. A channel is visible in the hydrophobic core, with dimensions of, 3 A x 9 A x 21 A. In some of the 20 solution structures calculated, this, channel is closed either by Trp-94 at one end or by Tyr-26 at the other, end; in some other solutions, this channel is closed at both ends. Binding, experiments with 12-bromododecanol indicate that the CSPMbraA6 structure, is modified upon ligand binding.
About this Structure
1K19 is a Single protein structure of sequence from Mamestra brassicae. Full crystallographic information is available from OCA.
Reference
Solution structure of a chemosensory protein from the moth Mamestra brassicae., Mosbah A, Campanacci V, Lartigue A, Tegoni M, Cambillau C, Darbon H, Biochem J. 2003 Jan 1;369(Pt 1):39-44. PMID:12217077
Page seeded by OCA on Sun Nov 25 00:32:45 2007
