2erb
From Proteopedia
(New page: 200px<br /><applet load="2erb" size="350" color="white" frame="true" align="right" spinBox="true" caption="2erb, resolution 1.50Å" /> '''AgamOBP1, and odoran...) |
|||
| Line 4: | Line 4: | ||
==Overview== | ==Overview== | ||
| - | The Anopheles gambiae mosquito is the main vector of malaria transmission | + | 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== | ==About this Structure== | ||
| Line 14: | Line 14: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Ishida, Y.]] | [[Category: Ishida, Y.]] | ||
| - | [[Category: Leal, W | + | [[Category: Leal, W S.]] |
[[Category: Morgan, T.]] | [[Category: Morgan, T.]] | ||
| - | [[Category: Wilson, D | + | [[Category: Wilson, D K.]] |
[[Category: Wogulis, M.]] | [[Category: Wogulis, M.]] | ||
[[Category: MG]] | [[Category: MG]] | ||
| Line 23: | Line 23: | ||
[[Category: helix]] | [[Category: helix]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:13:46 2008'' |
Revision as of 15:13, 21 February 2008
|
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
Page seeded by OCA on Thu Feb 21 17:13:46 2008
Categories: Anopheles gambiae | Single protein | Ishida, Y. | Leal, W S. | Morgan, T. | Wilson, D K. | Wogulis, M. | MG | PEU | Disulfides | Helix
