3pm2: Difference between revisions
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==Crystal structure of a novel type of odorant binding protein from Anopheles gambiae belonging to the c+ class== | |||
<StructureSection load='3pm2' size='340' side='right'caption='[[3pm2]], [[Resolution|resolution]] 1.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3pm2]] 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=3PM2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PM2 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]] 1.8Å</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=3pm2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pm2 OCA], [https://pdbe.org/3pm2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pm2 RCSB], [https://www.ebi.ac.uk/pdbsum/3pm2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pm2 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q7PF80_ANOGA Q7PF80_ANOGA] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Anopheles gambiae (Agam) relies on its olfactory system to target human prey, leading eventually to injection of Plasmodium falciparum, the malaria vector. Odorant-binding proteins (OBPs) are the first line of proteins involved in odorant recognition. They interact with olfactory receptors and thus constitute an interesting target for insect control. We undertook a large-scale study of proteins belonging to the olfactory system of Agam with the aim of preventing insect bites by designing strong olfactory repellents. We determined the 3D structures of several Agam OBPs alone or in complex with model compounds. Here, we report the first 3D structure of a member of the OBP C+ class, AgamOBP47, which has a longer sequence than classical OBPs and contains 6 disulphide bridges. AgamOBP47 possesses a core of six a-helices and three disulphide bridges, similar to the classical OBP fold. Two extra loops and the N- and C-terminal extra segments contain two additional a-helices and are maintained together by three disulphide bridges. They are embrace the classical OBP core domain. The binding site of OBP47 is located between the core and the additional domains. Two crevices are observed on opposite sides of OBP47, which are joined together by a shallow channel of sufficient size to accommodate a model of the best tested ligand. The binding sites of C+ class OBPs exhibit therefore different characteristics of their binding site, as compared to classical OBPs, which should leave to markedly diverse functional implications. | |||
Crystal structure of a novel type of odorant binding protein from Anopheles gambiae, belonging to the C+ class.,Lagarde A, Spinelli S, Qiao H, Tegoni M, Pelosi P, Cambillau C Biochem J. 2011 May 12. PMID:21561433<ref>PMID:21561433</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3pm2" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Odorant binding protein 3D structures|Odorant binding protein 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Anopheles gambiae]] | |||
[[Category: Large Structures]] | |||
[[Category: Cambillau C]] | |||
[[Category: Lagarde A]] | |||
[[Category: Pelosi P]] | |||
[[Category: Qiao H]] | |||
[[Category: Spinelli S]] | |||
[[Category: Tegoni M]] | |||
Latest revision as of 12:34, 30 October 2024
Crystal structure of a novel type of odorant binding protein from Anopheles gambiae belonging to the c+ classCrystal structure of a novel type of odorant binding protein from Anopheles gambiae belonging to the c+ class
Structural highlights
FunctionPublication Abstract from PubMedAnopheles gambiae (Agam) relies on its olfactory system to target human prey, leading eventually to injection of Plasmodium falciparum, the malaria vector. Odorant-binding proteins (OBPs) are the first line of proteins involved in odorant recognition. They interact with olfactory receptors and thus constitute an interesting target for insect control. We undertook a large-scale study of proteins belonging to the olfactory system of Agam with the aim of preventing insect bites by designing strong olfactory repellents. We determined the 3D structures of several Agam OBPs alone or in complex with model compounds. Here, we report the first 3D structure of a member of the OBP C+ class, AgamOBP47, which has a longer sequence than classical OBPs and contains 6 disulphide bridges. AgamOBP47 possesses a core of six a-helices and three disulphide bridges, similar to the classical OBP fold. Two extra loops and the N- and C-terminal extra segments contain two additional a-helices and are maintained together by three disulphide bridges. They are embrace the classical OBP core domain. The binding site of OBP47 is located between the core and the additional domains. Two crevices are observed on opposite sides of OBP47, which are joined together by a shallow channel of sufficient size to accommodate a model of the best tested ligand. The binding sites of C+ class OBPs exhibit therefore different characteristics of their binding site, as compared to classical OBPs, which should leave to markedly diverse functional implications. Crystal structure of a novel type of odorant binding protein from Anopheles gambiae, belonging to the C+ class.,Lagarde A, Spinelli S, Qiao H, Tegoni M, Pelosi P, Cambillau C Biochem J. 2011 May 12. PMID:21561433[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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