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<StructureSection load='2erb' size='340' side='right'caption='[[2erb]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
<StructureSection load='2erb' size='340' side='right'caption='[[2erb]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2erb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Anoga Anoga]. 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>
<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='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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</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>
<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>
</table>
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</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].
</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="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&reg;/PubMed&reg;, 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 3D structures|Odorant binding protein 3D structures]]
*[[Odorant binding protein 3D structures|Odorant binding protein 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Anoga]]
[[Category: Anopheles gambiae]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Ishida, Y]]
[[Category: Ishida Y]]
[[Category: Leal, W S]]
[[Category: Leal WS]]
[[Category: Morgan, T]]
[[Category: Morgan T]]
[[Category: Wilson, D K]]
[[Category: Wilson DK]]
[[Category: Wogulis, M]]
[[Category: Wogulis M]]
[[Category: Disulfide]]
[[Category: Helix]]
[[Category: Transport protein]]

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