7w61
From Proteopedia
(Difference between revisions)
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==Crystal structure of farnesol dehydrogenase from Helicoverpa armigera== | ==Crystal structure of farnesol dehydrogenase from Helicoverpa armigera== | ||
- | <StructureSection load='7w61' size='340' side='right'caption='[[7w61]]' scene=''> | + | <StructureSection load='7w61' size='340' side='right'caption='[[7w61]], [[Resolution|resolution]] 1.60Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7W61 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7W61 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7w61]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicoverpa_armigera Helicoverpa armigera]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7W61 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7W61 FirstGlance]. <br> |
- | </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=7w61 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7w61 OCA], [https://pdbe.org/7w61 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7w61 RCSB], [https://www.ebi.ac.uk/pdbsum/7w61 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7w61 ProSAT]</span></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</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=7w61 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7w61 OCA], [https://pdbe.org/7w61 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7w61 RCSB], [https://www.ebi.ac.uk/pdbsum/7w61 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7w61 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Farnesol dehydrogenase (FDL) orchestrates the oxidation reaction catalyzing farnesol to farnesal, a key step in the juvenile hormone (JH) biosynthesis pathway of insects and hence, represents a lucrative target for developing insect growth regulators (IGRs). However, information on the structural and functional characterization of JH-specific farnesol dehydrogenase in insects remains elusive. Herein, we identified a transcript that encodes farnesol dehydrogenase (HaFDL) from Helicoverpa armigera, a major pest of cotton. The investigations of molecular assembly, biochemical analysis and spatio-temporal expression profiling showed that HaFDL exists as a soluble homo-tetrameric form, exhibits a broad substrate affinity and is involved in the JH-specific farnesol oxidation in H. armigera. Additionally, the study presents the first crystal structure of the HaFDL-NADP enzyme complex determined at 1.6 A resolution. Structural analysis revealed that HaFDL belongs to the NADP-specific cP2 subfamily of the classical short-chain dehydrogenase/reductase (SDR) family and exhibits typical structural features of those enzymes including the conserved nucleotide-binding Rossman-fold. The isothermal titration calorimetry (ITC) showed a high binding affinity (dissociation constant, Kd, 3.43 muM) of NADP to the enzyme. Comparative structural analysis showed a distinct substrate-binding pocket (SBP) loop with a spacious and hydrophobic substrate-binding pocket in HaFDL, consistent with the biochemically observed promiscuous substrate specificity. Finally, based on the crystal structure, substrate modeling and structural comparison with homologs, a two-step reaction mechanism is proposed. Overall, the findings significantly impact and contribute to our understanding of farnesol dehydrogenase functional properties in JH biosynthesis in H. armigera. | ||
+ | |||
+ | Crystal structure and molecular characterization of NADP(+)-farnesol dehydrogenase from cotton bollworm, Helicoverpaarmigera.,Kumar R, Das J, Mahto JK, Sharma M, Vivek S, Kumar P, Sharma AK Insect Biochem Mol Biol. 2022 Jul 9;147:103812. doi: 10.1016/j.ibmb.2022.103812. PMID:35820537<ref>PMID:35820537</ref> | ||
+ | |||
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 7w61" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
+ | [[Category: Helicoverpa armigera]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Das J]] | [[Category: Das J]] |
Revision as of 04:18, 8 September 2022
Crystal structure of farnesol dehydrogenase from Helicoverpa armigera
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Categories: Helicoverpa armigera | Large Structures | Das J | Kumar P | Kumar R | Mahto JK | Sharma AK | Sharma M