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3vb1

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==Crystal Structure of Anopholes gambiae odorant binding protein 20 in open state==
==Crystal Structure of Anopholes gambiae odorant binding protein 20 in open state==
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<StructureSection load='3vb1' size='340' side='right' caption='[[3vb1]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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<StructureSection load='3vb1' size='340' side='right'caption='[[3vb1]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3vb1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Anopheles_gambiae Anopheles gambiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VB1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VB1 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3vb1]] is a 1 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=3VB1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VB1 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</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]] 2&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SME:METHIONINE+SULFOXIDE'>SME</scene></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=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=SME:METHIONINE+SULFOXIDE'>SME</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3v2l|3v2l]]</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=3vb1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vb1 OCA], [https://pdbe.org/3vb1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vb1 RCSB], [https://www.ebi.ac.uk/pdbsum/3vb1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vb1 ProSAT]</span></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">OBP20, AgaP_AGAP005208 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7165 Anopheles gambiae])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3vb1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vb1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vb1 RCSB], [http://www.ebi.ac.uk/pdbsum/3vb1 PDBsum]</span></td></tr>
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</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/Q7Q9J3_ANOGA Q7Q9J3_ANOGA]
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Anopheles gambiae mosquitoes that transmit malaria are attracted to humans by the odor molecules that emanate from skin and sweat. Odorant binding proteins (OBPs) are the first component of the olfactory apparatus to interact with odorant molecules, and so present potential targets for preventing transmission of malaria by disrupting the normal olfactory responses of the insect. AgamOBP20 is one of a limited subset of OBPs that it is preferentially expressed in female mosquitoes and its expression is regulated by blood feeding and by the day/night light cycles that correlate with blood-feeding behavior. Analysis of AgamOBP20 in solution reveals that the apo-protein exhibits significant conformational heterogeneity but the binding of odorant molecules results in a significant conformational change, which is accompanied by a reduction in the conformational flexibility present in the protein. Crystal structures of the free and bound states reveal a novel pathway for entrance and exit of odorant molecules into the central-binding pocket, and that the conformational changes associated with ligand binding are a result of rigid body domain motions in alpha-helices 1, 4 and 5, which act as lids to the binding pocket. These structures provide new insights into the specific residues involved in the conformational adaptation to different odorants and have important implications in the selection and development of reagents targeted at disrupting normal OBP function.
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A novel mechanism of ligand binding and release in the odorant binding protein 20 from the malaria mosquito Anopheles gambiae.,Ziemba BP, Murphy EJ, Edlin HT, Jones DN Protein Sci. 2012 Oct 18. doi: 10.1002/pro.2179. PMID:23081820<ref>PMID:23081820</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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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Anopheles gambiae]]
[[Category: Anopheles gambiae]]
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[[Category: Jones, D N]]
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[[Category: Large Structures]]
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[[Category: Ziemba, B P]]
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[[Category: Jones DN]]
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[[Category: Insect odorant-binding protein]]
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[[Category: Ziemba BP]]
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[[Category: None]]
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[[Category: Odor transport]]
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[[Category: Odorant-binding protein]]
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[[Category: Possible odorant receptor]]
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[[Category: Secreted lymph olfactory sensillum]]
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Current revision

Crystal Structure of Anopholes gambiae odorant binding protein 20 in open state

PDB ID 3vb1

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