7r0s: Difference between revisions
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==Structure of a cytosolic sulfotransferase of Anopheles gambiae (AGAP001425) in complex with vanillin== | |||
<StructureSection load='7r0s' size='340' side='right'caption='[[7r0s]], [[Resolution|resolution]] 2.10Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7r0s]] 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=7R0S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7R0S 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]] 2.1Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=V55:4-HYDROXY-3-METHOXYBENZALDEHYDE'>V55</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=7r0s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7r0s OCA], [https://pdbe.org/7r0s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7r0s RCSB], [https://www.ebi.ac.uk/pdbsum/7r0s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7r0s ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q7PXJ0_ANOGA Q7PXJ0_ANOGA] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The temporary or permanent chemical modification of biomolecules is a crucial aspect in the physiology of all living species. However, while some modules are well characterised also in insects, others did not receive the same attention. This holds true for sulfo-conjugation that is catalysed by cytosolic sulfotransferases (SULT), a central component of the metabolism of endogenous low molecular weight molecules and xenobiotics. In particular, limited information is available about the functional roles of the mosquito predicted enzymes annotated as SULTs in genomic databases. The herein described research is the first example of a biochemical and structural study of a SULT of a mosquito species, in general, and of the malaria vector Anopheles gambiae in particular. We confirmed that the AGAP001425 transcript displays a peculiar expression pattern that is suggestive of a possible involvement in modulating the mosquito reproductive tissues physiology, a fact that could raise attention on the enzyme as a potential target for insect-containment strategies. The crystal structures of the enzyme in alternative ligand-bound states revealed elements distinguishing AgSULT-001425 from other characterized SULTs, including a peculiar conformational plasticity of a discrete region that shields the catalytic cleft and that could play a main role in the dynamics of the reaction and in the substrate selectivity of the enzyme. Along with further in vitro biochemical studies, our structural investigations could provide a framework for the discovery of small-molecule inhibitors to assess the effect of interfering with AgSULT-001425-mediated catalysis at the organismal level. | |||
Biochemical and structural analysis of a cytosolic sulfotransferase of the malaria vector Anopheles gambiae overexpressed in the reproductive tissues.,Esposito Verza A, Miggiano R, Lombardo F, Fiorillo C, Arca B, Purghe B, Del Grosso E, Galli U, Rizzi M, Rossi F Curr Res Struct Biol. 2022 Jul 21;4:246-255. doi: 10.1016/j.crstbi.2022.07.001., eCollection 2022. PMID:35941867<ref>PMID:35941867</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 7r0s" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Sulfotransferase 3D structures|Sulfotransferase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Anopheles gambiae]] | |||
[[Category: Large Structures]] | |||
[[Category: Esposito Verza A]] | |||
[[Category: Miggiano R]] | |||
[[Category: Rizzi R]] | |||
[[Category: Rossi F]] | |||
Latest revision as of 16:25, 1 February 2024
Structure of a cytosolic sulfotransferase of Anopheles gambiae (AGAP001425) in complex with vanillinStructure of a cytosolic sulfotransferase of Anopheles gambiae (AGAP001425) in complex with vanillin
Structural highlights
FunctionPublication Abstract from PubMedThe temporary or permanent chemical modification of biomolecules is a crucial aspect in the physiology of all living species. However, while some modules are well characterised also in insects, others did not receive the same attention. This holds true for sulfo-conjugation that is catalysed by cytosolic sulfotransferases (SULT), a central component of the metabolism of endogenous low molecular weight molecules and xenobiotics. In particular, limited information is available about the functional roles of the mosquito predicted enzymes annotated as SULTs in genomic databases. The herein described research is the first example of a biochemical and structural study of a SULT of a mosquito species, in general, and of the malaria vector Anopheles gambiae in particular. We confirmed that the AGAP001425 transcript displays a peculiar expression pattern that is suggestive of a possible involvement in modulating the mosquito reproductive tissues physiology, a fact that could raise attention on the enzyme as a potential target for insect-containment strategies. The crystal structures of the enzyme in alternative ligand-bound states revealed elements distinguishing AgSULT-001425 from other characterized SULTs, including a peculiar conformational plasticity of a discrete region that shields the catalytic cleft and that could play a main role in the dynamics of the reaction and in the substrate selectivity of the enzyme. Along with further in vitro biochemical studies, our structural investigations could provide a framework for the discovery of small-molecule inhibitors to assess the effect of interfering with AgSULT-001425-mediated catalysis at the organismal level. Biochemical and structural analysis of a cytosolic sulfotransferase of the malaria vector Anopheles gambiae overexpressed in the reproductive tissues.,Esposito Verza A, Miggiano R, Lombardo F, Fiorillo C, Arca B, Purghe B, Del Grosso E, Galli U, Rizzi M, Rossi F Curr Res Struct Biol. 2022 Jul 21;4:246-255. doi: 10.1016/j.crstbi.2022.07.001., eCollection 2022. PMID:35941867[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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