6wle

From Proteopedia

(Difference between revisions)

Revision as of 14:30, 18 October 2023

Crystal structure of the Zeitlupe light-state mimic G46A

Structural highlights

6wle is a 7 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 3Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ADO1_ARATH Component of an E3 ubiquitin ligase complex that plays a central role in blue light-dependent circadian cycles. Acts as a blue light photoreceptor, due to the presence of FMN, that mediates light-regulated protein degradation of critical clock components by targeting them to the proteasome complex. The SCF(ADO1) E3 ubiquitin ligase complex is involved in the regulation of circadian clock-dependent processes including the transition to flowering time, hypocotyl elongation, cotyledons and leaf movement rhythms. APRR1/TOC1 and APRR5, but not 'GIGANTEA', are proteolytic substrates of this ubiquitin ligase complex. Blue light enhances cooperative stabilization of 'GIGANTEA' and ADO1/ZTL, leading to amplification and sharpening of the expression profile of APRR1/TOC1. ADO1/ZTL interacts with ADO3, preventing the interaction of ADO3 with CDF1.^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7] ^[8] ^[9]

Publication Abstract from PubMed

Plants measure light quality, intensity, and duration to coordinate growth and development with daily and seasonal changes in environmental conditions; however, the molecular details linking photochemistry to signal transduction remain incomplete. Two closely related light, oxygen, or voltage (LOV) domain-containing photoreceptor proteins, ZEITLUPE (ZTL) and FLAVIN-BINDING, KELCH REPEAT, F-BOX 1 (FKF1), divergently regulate the protein stability of circadian clock and photoperiodic flowering components to mediate daily and seasonal development. Using structural approaches, we identified that mutations at the Gly46 position led to global rearrangements of the ZTL dimer interface in the isolated ZTL-LOV domain. Specifically, G46S and G46A variants induce a 180 degrees rotation about the ZTL-LOV dimer interface that is coupled to ordering of N- and C-terminal signaling elements. These conformational changes hinge upon rotation of a C-terminal Gln residue (Gln154) analogous to that present in light-state structures of ZTL. In contrast to other LOV proteins, a Q154L variant retains light-state interactions with GIGANTEA (GI), thereby indicating N5 protonation is not required for ZTL signaling. The results presented herein confirm a divergent signaling mechanism within ZTL, whereby steric and electronic effects following adduct formation can be sufficient for signal propagation in LOV proteins containing a Gly residue at position 46. Examination of bacterial LOV structures with Gly residues at the equivalent position suggests that mechanisms of signal transduction in LOV proteins may be fluid across the LOV protein family.

Steric and Electronic Interactions at Gln154 in ZEITLUPE Induce Reorganization of the LOV Domain Dimer Interface.,Pudasaini A, Green R, Song YH, Blumenfeld A, Karki N, Imaizumi T, Zoltowski BD Biochemistry. 2021 Jan 19;60(2):95-103. doi: 10.1021/acs.biochem.0c00819. Epub, 2020 Dec 18. PMID:33337855^[10]

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

References

↑ Somers DE, Schultz TF, Milnamow M, Kay SA. ZEITLUPE encodes a novel clock-associated PAS protein from Arabidopsis. Cell. 2000 Apr 28;101(3):319-29. PMID:10847686
↑ Nelson DC, Lasswell J, Rogg LE, Cohen MA, Bartel B. FKF1, a clock-controlled gene that regulates the transition to flowering in Arabidopsis. Cell. 2000 Apr 28;101(3):331-40. PMID:10847687
↑ Kiyosue T, Wada M. LKP1 (LOV kelch protein 1): a factor involved in the regulation of flowering time in arabidopsis. Plant J. 2000 Sep;23(6):807-15. PMID:10998191
↑ Jarillo JA, Capel J, Tang RH, Yang HQ, Alonso JM, Ecker JR, Cashmore AR. An Arabidopsis circadian clock component interacts with both CRY1 and phyB. Nature. 2001 Mar 22;410(6827):487-90. PMID:11260718 doi:http://dx.doi.org/10.1038/35068589
↑ Somers DE, Kim WY, Geng R. The F-box protein ZEITLUPE confers dosage-dependent control on the circadian clock, photomorphogenesis, and flowering time. Plant Cell. 2004 Mar;16(3):769-82. Epub 2004 Feb 18. PMID:14973171 doi:http://dx.doi.org/10.1105/tpc.016808
↑ Han L, Mason M, Risseeuw EP, Crosby WL, Somers DE. Formation of an SCF(ZTL) complex is required for proper regulation of circadian timing. Plant J. 2004 Oct;40(2):291-301. PMID:15447654 doi:http://dx.doi.org/10.1111/j.1365-313X.2004.02207.x
↑ Kevei E, Gyula P, Hall A, Kozma-Bognar L, Kim WY, Eriksson ME, Toth R, Hanano S, Feher B, Southern MM, Bastow RM, Viczian A, Hibberd V, Davis SJ, Somers DE, Nagy F, Millar AJ. Forward genetic analysis of the circadian clock separates the multiple functions of ZEITLUPE. Plant Physiol. 2006 Mar;140(3):933-45. Epub 2006 Jan 20. PMID:16428597 doi:http://dx.doi.org/10.1104/pp.105.074864
↑ Kim WY, Fujiwara S, Suh SS, Kim J, Kim Y, Han L, David K, Putterill J, Nam HG, Somers DE. ZEITLUPE is a circadian photoreceptor stabilized by GIGANTEA in blue light. Nature. 2007 Sep 20;449(7160):356-60. Epub 2007 Aug 19. PMID:17704763 doi:http://dx.doi.org/10.1038/nature06132
↑ Takase T, Nishiyama Y, Tanihigashi H, Ogura Y, Miyazaki Y, Yamada Y, Kiyosue T. LOV KELCH PROTEIN2 and ZEITLUPE repress Arabidopsis photoperiodic flowering under non-inductive conditions, dependent on FLAVIN-BINDING KELCH REPEAT F-BOX1. Plant J. 2011 Aug;67(4):608-21. doi: 10.1111/j.1365-313X.2011.04618.x. Epub 2011 , Jul 14. PMID:21518052 doi:http://dx.doi.org/10.1111/j.1365-313X.2011.04618.x
↑ Pudasaini A, Green R, Song YH, Blumenfeld A, Karki N, Imaizumi T, Zoltowski BD. Steric and Electronic Interactions at Gln154 in ZEITLUPE Induce Reorganization of the LOV Domain Dimer Interface. Biochemistry. 2021 Jan 19;60(2):95-103. PMID:33337855 doi:10.1021/acs.biochem.0c00819

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

Categories: Arabidopsis thaliana | Large Structures | Green R | Zoltowski B

@@ Line 1: / Line 1: @@
 ==Crystal structure of the Zeitlupe light-state mimic G46A==
-<StructureSection load='6wle' size='340' side='right'caption='[[6wle]]' scene=''>
+<StructureSection load='6wle' size='340' side='right'caption='[[6wle]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6WLE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6WLE FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6wle]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6WLE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6WLE 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=6wle FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6wle OCA], [https://pdbe.org/6wle PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6wle RCSB], [https://www.ebi.ac.uk/pdbsum/6wle PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6wle ProSAT]</span></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]] 3&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</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=6wle FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6wle OCA], [https://pdbe.org/6wle PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6wle RCSB], [https://www.ebi.ac.uk/pdbsum/6wle PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6wle ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/ADO1_ARATH ADO1_ARATH] Component of an E3 ubiquitin ligase complex that plays a central role in blue light-dependent circadian cycles. Acts as a blue light photoreceptor, due to the presence of FMN, that mediates light-regulated protein degradation of critical clock components by targeting them to the proteasome complex. The SCF(ADO1) E3 ubiquitin ligase complex is involved in the regulation of circadian clock-dependent processes including the transition to flowering time, hypocotyl elongation, cotyledons and leaf movement rhythms. APRR1/TOC1 and APRR5, but not 'GIGANTEA', are proteolytic substrates of this ubiquitin ligase complex. Blue light enhances cooperative stabilization of 'GIGANTEA' and ADO1/ZTL, leading to amplification and sharpening of the expression profile of APRR1/TOC1. ADO1/ZTL interacts with ADO3, preventing the interaction of ADO3 with CDF1.<ref>PMID:10847686</ref> <ref>PMID:10847687</ref> <ref>PMID:10998191</ref> <ref>PMID:11260718</ref> <ref>PMID:14973171</ref> <ref>PMID:15447654</ref> <ref>PMID:16428597</ref> <ref>PMID:17704763</ref> <ref>PMID:21518052</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Plants measure light quality, intensity, and duration to coordinate growth and development with daily and seasonal changes in environmental conditions; however, the molecular details linking photochemistry to signal transduction remain incomplete. Two closely related light, oxygen, or voltage (LOV) domain-containing photoreceptor proteins, ZEITLUPE (ZTL) and FLAVIN-BINDING, KELCH REPEAT, F-BOX 1 (FKF1), divergently regulate the protein stability of circadian clock and photoperiodic flowering components to mediate daily and seasonal development. Using structural approaches, we identified that mutations at the Gly46 position led to global rearrangements of the ZTL dimer interface in the isolated ZTL-LOV domain. Specifically, G46S and G46A variants induce a 180 degrees rotation about the ZTL-LOV dimer interface that is coupled to ordering of N- and C-terminal signaling elements. These conformational changes hinge upon rotation of a C-terminal Gln residue (Gln154) analogous to that present in light-state structures of ZTL. In contrast to other LOV proteins, a Q154L variant retains light-state interactions with GIGANTEA (GI), thereby indicating N5 protonation is not required for ZTL signaling. The results presented herein confirm a divergent signaling mechanism within ZTL, whereby steric and electronic effects following adduct formation can be sufficient for signal propagation in LOV proteins containing a Gly residue at position 46. Examination of bacterial LOV structures with Gly residues at the equivalent position suggests that mechanisms of signal transduction in LOV proteins may be fluid across the LOV protein family.
+Steric and Electronic Interactions at Gln154 in ZEITLUPE Induce Reorganization of the LOV Domain Dimer Interface.,Pudasaini A, Green R, Song YH, Blumenfeld A, Karki N, Imaizumi T, Zoltowski BD Biochemistry. 2021 Jan 19;60(2):95-103. doi: 10.1021/acs.biochem.0c00819. Epub, 2020 Dec 18. PMID:33337855<ref>PMID:33337855</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 6wle" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
 __TOC__
 </StructureSection>
+[[Category: Arabidopsis thaliana]]
 [[Category: Large Structures]]
 [[Category: Green R]]
 [[Category: Zoltowski B]]

6wle

From Proteopedia

Revision as of 14:30, 18 October 2023

Crystal structure of the Zeitlupe light-state mimic G46A

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox