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==AgamOBP1, and odorant binding protein from Anopheles gambiae complexed with PEG== | |||
<StructureSection load='2erb' size='340' side='right'caption='[[2erb]], [[Resolution|resolution]] 1.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2erb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Anopheles_gambiae Anopheles gambiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ERB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ERB FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2erb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2erb OCA], [https://pdbe.org/2erb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2erb RCSB], [https://www.ebi.ac.uk/pdbsum/2erb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2erb ProSAT]</span></td></tr> | |||
</table> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/er/2erb_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2erb ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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<ref>PMID:16300742</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2erb" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Odorant binding protein|Odorant binding protein]] | *[[Odorant binding protein 3D structures|Odorant binding protein 3D structures]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Anopheles gambiae]] | [[Category: Anopheles gambiae]] | ||
[[Category: Ishida | [[Category: Large Structures]] | ||
[[Category: Leal | [[Category: Ishida Y]] | ||
[[Category: Morgan | [[Category: Leal WS]] | ||
[[Category: Wilson | [[Category: Morgan T]] | ||
[[Category: Wogulis | [[Category: Wilson DK]] | ||
[[Category: Wogulis M]] | |||
Latest revision as of 03:53, 21 November 2024
AgamOBP1, and odorant binding protein from Anopheles gambiae complexed with PEGAgamOBP1, and odorant binding protein from Anopheles gambiae complexed with PEG
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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