2erb: Difference between revisions

Revision as of 03:40, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2erb.png

Template:STRUCTURE 2erb

AgamOBP1, and odorant binding protein from Anopheles gambiae complexed with PEGAgamOBP1, and odorant binding protein from Anopheles gambiae complexed with PEG

Template:ABSTRACT PUBMED 16300742

About this StructureAbout this Structure

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

ReferenceReference

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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OCA

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+===AgamOBP1, and odorant binding protein from Anopheles gambiae complexed with PEG===
-==Overview==
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-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.
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