1K19
NMR Solution Structure of the Chemosensory Protein CSP2 from Moth Mamestra brassicae
Summary for 1K19
| Entry DOI | 10.2210/pdb1k19/pdb |
| NMR Information | BMRB: 5094 |
| Descriptor | Chemosensory Protein CSP2 (1 entity in total) |
| Functional Keywords | chemosensory, pheromone, lipid transport |
| Biological source | Mamestra brassicae (cabbage moth) |
| Total number of polymer chains | 1 |
| Total formula weight | 13094.84 |
| 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 citation | Mosbah, 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: 12217077DOI: 10.1042/BJ20021217 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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