1xfr

Solution structure of the Bombyx mori pheromone-binding protein fragment BmPBP(1-128) at pH 6.5

spinqualitylabelsall models 1xfr, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1xfr is a 1 chain structure with sequence from Bommo. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1ls8, 1dqe, 1gm0 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [PBP_BOMMO] This major soluble protein in olfactory sensilla of male moths serves to solubilize the extremely hydrophobic pheromone molecules such as bombykol and to transport pheromone through the aqueous lymph to receptors located on olfactory cilia. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The Bombyx mori pheromone-binding protein (BmorPBP) undergoes a pH-dependent conformational transition from a form at basic pH, which contains an open cavity suitable for ligand binding (BmorPBP(B)), to a form at pH 4.5, where this cavity is occupied by an additional helix (BmorPBP(A)). This helix alpha7 is formed by the C-terminal dodecapeptide 131-142, which is flexibly disordered on the protein surface in BmorPBP(B) and in its complex with the pheromone bombykol. Previous work showed that the ligand-binding cavity cannot accommodate both bombykol and helix alpha7. Here we further investigated mechanistic aspects of the physiologically crucial ejection of the ligand at lower pH values by solution NMR studies of the variant protein BmorPBP(1-128), where the C-terminal helix-forming tetradecapeptide is removed. The NMR structure of the truncated protein at pH 6.5 corresponds closely to BmorPBP(B). At pH 4.5, BmorPBP(1-128) maintains a B-type structure that is in a slow equilibrium, on the NMR chemical shift timescale, with a low-pH conformation for which a discrete set of (15)N-(1)H correlation peaks is NMR unobservable. The full NMR spectrum was recovered upon readjusting the pH of the protein solution to 6.5. These data reveal dual roles for the C-terminal tetradecapeptide of BmorPBP in the mechanism of reversible pheromone binding and transport, where it governs dynamic equilibria between two locally different protein conformations at acidic pH and competes with the ligand for binding to the interior cavity. Dynamic conformational equilibria in the physiological function of the Bombyx mori pheromone-binding protein.,Michel E, Damberger FF, Ishida Y, Fiorito F, Lee D, Leal WS, Wuthrich K J Mol Biol. 2011 May 20;408(5):922-31. Epub 2011 Mar 17. PMID:21396939 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Pheromone binding protein

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