1KX8
Antennal Chemosensory Protein A6 from Mamestra brassicae, tetragonal form
Summary for 1KX8
| Entry DOI | 10.2210/pdb1kx8/pdb |
| Related | 1KX9 |
| Descriptor | CHEMOSENSORY PROTEIN A6 (2 entities in total) |
| Functional Keywords | all helix, lipid transport |
| Biological source | Mamestra brassicae (cabbage moth) |
| Total number of polymer chains | 1 |
| Total formula weight | 13094.84 |
| Authors | Lartigue, A.,Campanacci, V.,Roussel, A.,Larsson, A.M.,Jones, T.A.,Tegoni, M.,Cambillau, C. (deposition date: 2002-01-31, release date: 2002-12-04, Last modification date: 2024-10-30) |
| Primary citation | Lartigue, A.,Campanacci, V.,Roussel, A.,Larsson, A.M.,Jones, T.A.,Tegoni, M.,Cambillau, C. X-Ray Structure and Ligand Binding Study of a Chemosensory Protein J.Biol.Chem., 277:32094-32098, 2002 Cited by PubMed Abstract: Chemosensory proteins (CSPs) are believed to be involved in chemical communication and perception. Such proteins, of M(r) 13,000, have been isolated from several sensory organs of a wide range of insect species. Several CSPs have been identified in the antennae and proboscis of the moth Mamestra brassicae. One of them, CSPMbraA6, a 112-amino acid antennal protein, has been expressed in large quantities and is soluble in the Escherichia coli periplasm. X-ray structure determination has been performed in parallel with ligand binding assays using tryptophan fluorescence quenching. The protein has overall dimensions of 25 x 30 x 32 A and exhibits a novel type of alpha-helical fold with six helices connected by alpha-alpha loops. A narrow channel extends within the protein hydrophobic core. Fluorescence quenching with brominated alkyl alcohols or fatty acids and modeling studies indicates that CSPMbraA6 is able to bind such compounds with C12-18 alkyl chains. These ubiquitous proteins might have the role of extracting hydrophobic linear compounds (pheromones, odors, or fatty acids) dispersed in the phospholipid membrane and transporting them to their receptor. PubMed: 12068017DOI: 10.1074/jbc.M204371200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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