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2erb

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[[Image:2erb.gif|left|200px]]
[[Image:2erb.gif|left|200px]]
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{{Structure
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|PDB= 2erb |SIZE=350|CAPTION= <scene name='initialview01'>2erb</scene>, resolution 1.50&Aring;
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The line below this paragraph, containing "STRUCTURE_2erb", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PEU:2,5,8,11,14,17,20,23,26,29,32,35,38,41,44,47,50,53,56,59,62,65,68,71,74,77,80-HEPTACOSAOXADOOCTACONTAN-82-OL'>PEU</scene>
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{{STRUCTURE_2erb| PDB=2erb | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2erb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2erb OCA], [http://www.ebi.ac.uk/pdbsum/2erb PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2erb RCSB]</span>
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'''AgamOBP1, and odorant binding protein from Anopheles gambiae complexed with PEG'''
'''AgamOBP1, and odorant binding protein from Anopheles gambiae complexed with PEG'''
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[[Category: Wilson, D K.]]
[[Category: Wilson, D K.]]
[[Category: Wogulis, M.]]
[[Category: Wogulis, M.]]
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[[Category: disulfide]]
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[[Category: Disulfide]]
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[[Category: helix]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:01:47 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:52:45 2008''
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Revision as of 00:01, 4 May 2008

Template:STRUCTURE 2erb

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. 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 Page seeded by OCA on Sun May 4 03:01:47 2008

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