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6keq

From Proteopedia

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Crystal structure of D113A mutant of Drosophila melanogaster Noppera-bo, glutathione S-transferase epsilon 14 (DmGSTE14), in apo-form

Structural highlights

6keq is a 2 chain structure with sequence from Drosophila melanogaster. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.84Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GSTEE_DROME Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles (PubMed:22082028). Essential for ecdysteroid biosynthesis (PubMed:25344753, PubMed:25300303). May be involved in detoxification (PubMed:22082028).^[1] ^[2] ^[3]

Publication Abstract from PubMed

Ecdysteroids are the principal steroid hormones essential for insect development and physiology. In the last 18 years, several enzymes responsible for ecdysteroid biosynthesis encoded by Halloween genes were identified and genetically and biochemically characterized. However, the tertiary structures of these proteins have not yet been characterized. Here, we report the results of an integrated series of in silico, in vitro, and in vivo analyses of the Halloween GST protein Noppera-bo (Nobo). We determined crystal structures of Drosophila melanogaster Nobo (DmNobo) complexed with glutathione and 17beta-estradiol, a DmNobo inhibitor. 17beta-Estradiol almost fully occupied the putative ligand-binding pocket and a prominent hydrogen bond formed between 17beta-estradiol and Asp-113 of DmNobo. We found that Asp-113 is essential for 17beta-estradiol-mediated inhibition of DmNobo enzymatic activity, as 17beta-estradiol did not inhibit and physically interacted less with the D113A DmNobo variant. Asp-113 is highly conserved among Nobo proteins, but not among other GSTs, implying that this residue is important for endogenous Nobo function. Indeed, a homozygous nobo allele with the D113A substitution exhibited embryonic lethality and an undifferentiated cuticle structure, a phenocopy of complete loss-of-function nobo homozygotes. These results suggest that the nobo family of GST proteins has acquired a unique amino acid residue that appears to be essential for binding an endogenous sterol substrate to regulate ecdysteroid biosynthesis. To the best of our knowledge, ours is the first study describing the structural characteristics of insect steroidogenic Halloween proteins. Our findings provide insights relevant for applied entomology to develop insecticides that specifically inhibit ecdysteroid biosynthesis.

An integrated approach to unravel a crucial structural property required for the function of the insect steroidogenic Halloween protein Noppera-bo.,Koiwai K, Inaba K, Morohashi K, Enya S, Arai R, Kojima H, Okabe T, Fujikawa Y, Inoue H, Yoshino R, Hirokawa T, Kato K, Fukuzawa K, Shimada-Niwa Y, Nakamura A, Yumoto F, Senda T, Niwa R J Biol Chem. 2020 Apr 2. pii: RA119.011463. doi: 10.1074/jbc.RA119.011463. PMID:32241910^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Saisawang C, Wongsantichon J, Ketterman AJ. A preliminary characterization of the cytosolic glutathione transferase proteome from Drosophila melanogaster. Biochem J. 2012 Feb 15;442(1):181-90. doi: 10.1042/BJ20111747. PMID:22082028 doi:http://dx.doi.org/10.1042/BJ20111747
↑ Enya S, Ameku T, Igarashi F, Iga M, Kataoka H, Shinoda T, Niwa R. A Halloween gene noppera-bo encodes a glutathione S-transferase essential for ecdysteroid biosynthesis via regulating the behaviour of cholesterol in Drosophila. Sci Rep. 2014 Oct 10;4:6586. doi: 10.1038/srep06586. PMID:25300303 doi:http://dx.doi.org/10.1038/srep06586
↑ Chanut-Delalande H, Hashimoto Y, Pelissier-Monier A, Spokony R, Dib A, Kondo T, Bohere J, Niimi K, Latapie Y, Inagaki S, Dubois L, Valenti P, Polesello C, Kobayashi S, Moussian B, White KP, Plaza S, Kageyama Y, Payre F. Pri peptides are mediators of ecdysone for the temporal control of development. Nat Cell Biol. 2014 Nov;16(11):1035-44. doi: 10.1038/ncb3052. Epub 2014 Oct 26. PMID:25344753 doi:http://dx.doi.org/10.1038/ncb3052
↑ Koiwai K, Inaba K, Morohashi K, Enya S, Arai R, Kojima H, Okabe T, Fujikawa Y, Inoue H, Yoshino R, Hirokawa T, Kato K, Fukuzawa K, Shimada-Niwa Y, Nakamura A, Yumoto F, Senda T, Niwa R. An integrated approach to unravel a crucial structural property required for the function of the insect steroidogenic Halloween protein Noppera-bo. J Biol Chem. 2020 Apr 2. pii: RA119.011463. doi: 10.1074/jbc.RA119.011463. PMID:32241910 doi:http://dx.doi.org/10.1074/jbc.RA119.011463

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6keq"

@@ Line 3: / Line 3: @@
 <StructureSection load='6keq' size='340' side='right'caption='[[6keq]], [[Resolution|resolution]] 1.84&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6keq]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KEQ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6KEQ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6keq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KEQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6KEQ FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GstE14, GSTD14-14, nobo, CG4688 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.84&#8491;</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] </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=6keq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6keq OCA], [https://pdbe.org/6keq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6keq RCSB], [https://www.ebi.ac.uk/pdbsum/6keq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6keq ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6keq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6keq OCA], [http://pdbe.org/6keq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6keq RCSB], [http://www.ebi.ac.uk/pdbsum/6keq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6keq ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/GSTEE_DROME GSTEE_DROME]] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles (PubMed:22082028). Essential for ecdysteroid biosynthesis (PubMed:25344753, PubMed:25300303). May be involved in detoxification (PubMed:22082028).<ref>PMID:22082028</ref> <ref>PMID:25300303</ref> <ref>PMID:25344753</ref>
+[https://www.uniprot.org/uniprot/GSTEE_DROME GSTEE_DROME] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles (PubMed:22082028). Essential for ecdysteroid biosynthesis (PubMed:25344753, PubMed:25300303). May be involved in detoxification (PubMed:22082028).<ref>PMID:22082028</ref> <ref>PMID:25300303</ref> <ref>PMID:25344753</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 19: / Line 18: @@
 </div>
 <div class="pdbe-citations 6keq" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Drome]]
+[[Category: Drosophila melanogaster]]
-[[Category: Glutathione transferase]]
 [[Category: Large Structures]]
-[[Category: Inaba, K]]
+[[Category: Inaba K]]
-[[Category: Koiwai, K]]
+[[Category: Koiwai K]]
-[[Category: Morohashi, K]]
+[[Category: Morohashi K]]
-[[Category: Niwa, R]]
+[[Category: Niwa R]]
-[[Category: Senda, T]]
+[[Category: Senda T]]
-[[Category: Yumoto, F]]
+[[Category: Yumoto F]]
-[[Category: Glutathione]]
-[[Category: Glutathione s-transferase]]
-[[Category: Gst]]
-[[Category: Transferase]]

6keq

From Proteopedia

Current revision

Crystal structure of D113A mutant of Drosophila melanogaster Noppera-bo, glutathione S-transferase epsilon 14 (DmGSTE14), in apo-form

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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