2erb
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 2erb |SIZE=350|CAPTION= <scene name='initialview01'>2erb</scene>, resolution 1.50Å | |PDB= 2erb |SIZE=350|CAPTION= <scene name='initialview01'>2erb</scene>, resolution 1.50Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> | + | |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> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |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> | ||
}} | }} | ||
| Line 27: | Line 30: | ||
[[Category: Wilson, D K.]] | [[Category: Wilson, D K.]] | ||
[[Category: Wogulis, M.]] | [[Category: Wogulis, M.]] | ||
| - | [[Category: MG]] | ||
| - | [[Category: PEU]] | ||
[[Category: disulfide]] | [[Category: disulfide]] | ||
[[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 Mon Mar 31 02:52:45 2008'' |
Revision as of 23:52, 30 March 2008
| |||||||
| , resolution 1.50Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Mon Mar 31 02:52:45 2008
