3r1p

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<StructureSection load='3r1p' size='340' side='right'caption='[[3r1p]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
<StructureSection load='3r1p' size='340' side='right'caption='[[3r1p]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3r1p]] is a 6 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=3R1P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3R1P FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3r1p]] is a 6 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=3R1P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3R1P FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3r1o|3r1o]], [[3r1v|3r1v]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">OBP7, AgamOBP7, AGAP001556, agCG57323 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7165 ANOGA])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3r1p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r1p OCA], [https://pdbe.org/3r1p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3r1p RCSB], [https://www.ebi.ac.uk/pdbsum/3r1p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3r1p 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=3r1p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r1p OCA], [https://pdbe.org/3r1p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3r1p RCSB], [https://www.ebi.ac.uk/pdbsum/3r1p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3r1p ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q7PXT9_ANOGA Q7PXT9_ANOGA]
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Anopheles gambiae (Agam) targets human and animals by using its olfactory system, leading to the spread of Plasmodium falciparum, the malaria vector. Odorant binding proteins (OBPs) participate to the first event in odorant recognition and constitute an interesting target for insect control. OBPs interact with olfactory receptors to which they deliver the odorant molecule. We have undertaken a large-scale study of proteins belonging to the olfactory system of Agam with in mind of designing strong olfactory repellants. Here, we report the expression, three-dimensional structures and binding properties of AgamOBP07, a member of a new structural class of OBPs, characterized by the occurrence of eight cysteines. We showed that AgamOBP07 possesses seven alpha-helices and four disulfide bridges, instead of six alpha-helices and three disulfide bridges in classical OBPs. The extra seventh helix is located at the surface of the protein, locked by the fourth disulfide bridge, and forms a wall of the internal cavity. The binding site of the protein is mainly hydrophobic, elongated and open and is able to accommodate elongated ligands, linear or polycyclic, as suggested also by binding experiments. An elongated electron density was observed in the internal cavity of the purified protein, belonging to a serendipitous ligand. The structure of AgamOBP07 in complex with an azo-bicyclic model compound reveals that a large conformational change in the protein has reshaped its binding site, provoking helix 4 unfolding and doubling of the cavity volume.
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The Crystal Structure of Odorant Binding Protein 7 from Anopheles gambiae Exhibits an Outstanding Adaptability of Its Binding Site.,Lagarde A, Spinelli S, Tegoni M, He X, Field L, Zhou JJ, Cambillau C J Mol Biol. 2011 Oct 12. PMID:22019737<ref>PMID:22019737</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3r1p" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Odorant binding protein 3D structures|Odorant binding protein 3D structures]]
*[[Odorant binding protein 3D structures|Odorant binding protein 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Anoga]]
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[[Category: Anopheles gambiae]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Cambillau, C]]
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[[Category: Cambillau C]]
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[[Category: Field, L]]
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[[Category: Field L]]
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[[Category: He, X]]
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[[Category: He X]]
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[[Category: Lagarde, A]]
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[[Category: Lagarde A]]
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[[Category: Spinelli, S]]
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[[Category: Spinelli S]]
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[[Category: Tegoni, M]]
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[[Category: Tegoni M]]
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[[Category: Zhou, J J]]
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[[Category: Zhou JJ]]
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[[Category: All helical protein]]
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[[Category: Mosquito antenna]]
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[[Category: Odorant molecules binding]]
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[[Category: Transport protein]]
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Revision as of 12:06, 14 March 2024

Odorant Binding Protein 7 from Anopheles gambiae with Four Disulfide Bridges, form P1

PDB ID 3r1p

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