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1K19

NMR Solution Structure of the Chemosensory Protein CSP2 from Moth Mamestra brassicae

Summary for 1K19
Entry DOI10.2210/pdb1k19/pdb
NMR InformationBMRB: 5094
DescriptorChemosensory Protein CSP2 (1 entity in total)
Functional Keywordschemosensory, pheromone, lipid transport
Biological sourceMamestra brassicae (cabbage moth)
Total number of polymer chains1
Total formula weight13094.84
Authors
Mosbah, A.,Campanacci, V.,Lartigue, A.,Tegoni, M.,Cambillau, C.,Darbon, H. (deposition date: 2001-09-24, release date: 2002-12-04, Last modification date: 2024-11-13)
Primary citationMosbah, A.,Campanacci, V.,Lartigue, A.,Tegoni, M.,Cambillau, C.,Darbon, H.
Solution structure of a chemosensory protein from the moth Mamestra brassicae
BIOCHEM.J., 369:39-44, 2003
Cited by
PubMed Abstract: 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.
PubMed: 12217077
DOI: 10.1042/BJ20021217
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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