2erb

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Revision as of 17:19, 29 January 2008

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spinqualitylabelsall models 2erb, resolution 1.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

AgamOBP1, and odorant binding protein from Anopheles gambiae complexed with PEG

Overview

The Anopheles gambiae mosquito is the main vector of malaria transmission, in sub-Saharan Africa. We present here a 1.5A crystal structure of, AgamOBP1, an odorant binding protein (OBP) from the A. gambiae mosquito., The protein crystallized as a dimer with a unique binding pocket, consisting of a continuous tunnel running through both subunits of the, dimer and occupied by a PEG molecule. We demonstrate that AgamOBP1, undergoes a pH dependent conformational change that is associated with, reduced ligand binding. A predominance of acid-labile hydrogen bonds, involving the C-terminal loop suggests a mechanism in which a drop in pH, causes C-terminal loop to open, leaving the binding tunnel solvent, exposed, thereby lowering binding affinity for ligand. Because proteins, from two distantly related insects also undergo a pH dependent, conformational change involving the C-terminus that is associated with, reduced ligand affinity, our results suggest a common mechanism for OBP, activity.

About this Structure

2ERB is a Single protein structure of sequence from Anopheles gambiae with and as ligands. Full crystallographic information is available from OCA.

Reference

The crystal structure of an odorant binding protein from Anopheles gambiae: evidence for a common ligand release mechanism., Wogulis M, Morgan T, Ishida Y, Leal WS, Wilson DK, Biochem Biophys Res Commun. 2006 Jan 6;339(1):157-64. Epub 2005 Nov 9. PMID:16300742

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