8zq4

From Proteopedia

(Difference between revisions)

Current revision

Structure of the Arabidopsis ABCB1 EQ mutant in the BL plus ATP bound state

Structural highlights

8zq4 is a 1 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:	Electron Microscopy, Resolution 3.8Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

AB1B_ARATH Auxin efflux transporter that acts as a negative regulator of light signaling to promote hypocotyl elongation. Mediates the accumulation of chlorophyll and anthocyanin, as well as the expression of genes in response to light. Participates directly in auxin efflux and thus regulates the polar (presumably basipetal) auxin transport (from root tips to root elongating zone). Transports also some auxin metabolites such as oxindoleacetic acid and indoleacetaldehyde. Involved in diverse auxin-mediated responses including gravitropism, phototropism and lateral root formation. Confers resistance to herbicides such as dicamba, pendimethalin, oryzalin, and monosodium acid methanearsonate (MSMA), but not to herbicides such as glyphosate, atrazine, bentazon and fluazifop-p-butyl. Mediates also resistance to xenobiotics such as cycloheximide and the cytokinin N6-(2-isopentenyl)adenine (2IP).^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7]

Publication Abstract from PubMed

Brassinosteroids (BRs) are steroidal phytohormones indispensable for plant growth, development, and responses to environmental stresses. The export of bioactive BRs to the apoplast is essential for BR signaling initiation, which requires binding of a BR molecule to the extracellular domains of the plasma membrane-localized receptor complex. We have previously shown that the Arabidopsis thaliana ATP-binding cassette (ABC) transporter ABCB19 functions as a BR exporter and, together with its close homolog ABCB1, positively regulates BR signaling. Here, we demonstrate that ABCB1 is another BR transporter. The ATP hydrolysis activity of ABCB1 can be stimulated by bioactive BRs, and its transport activity was confirmed in proteoliposomes and protoplasts. Structures of ABCB1 were determined in substrate-unbound (apo), brassinolide (BL)-bound, and ATP plus BL-bound states. In the BL-bound structure, BL is bound to the hydrophobic cavity formed by the transmembrane domain and triggers local conformational changes. Together, our data provide additional insights into ABC transporter-mediated BR export.

Structural insights into brassinosteroid export mediated by the Arabidopsis ABC transporter ABCB1.,Wei H, Zhu H, Ying W, Janssens H, Kvasnica M, Winne JM, Gao Y, Friml J, Ma Q, Tan S, Liu X, Russinova E, Sun L Plant Commun. 2025 Jan 13;6(1):101181. doi: 10.1016/j.xplc.2024.101181. Epub 2024 , Nov 4. PMID:39497419^[8]

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

References

↑ Thomas C, Rajagopal A, Windsor B, Dudler R, Lloyd A, Roux SJ. A role for ectophosphatase in xenobiotic resistance. Plant Cell. 2000 Apr;12(4):519-33. PMID:10760241 doi:10.1105/tpc.12.4.519
↑ Noh B, Murphy AS, Spalding EP. Multidrug resistance-like genes of Arabidopsis required for auxin transport and auxin-mediated development. Plant Cell. 2001 Nov;13(11):2441-54. PMID:11701880 doi:10.1105/tpc.010350
↑ Windsor B, Roux SJ, Lloyd A. Multiherbicide tolerance conferred by AtPgp1 and apyrase overexpression in Arabidopsis thaliana. Nat Biotechnol. 2003 Apr;21(4):428-33. PMID:12640467 doi:10.1038/nbt809
↑ Geisler M, Kolukisaoglu HU, Bouchard R, Billion K, Berger J, Saal B, Frangne N, Koncz-Kalman Z, Koncz C, Dudler R, Blakeslee JJ, Murphy AS, Martinoia E, Schulz B. TWISTED DWARF1, a unique plasma membrane-anchored immunophilin-like protein, interacts with Arabidopsis multidrug resistance-like transporters AtPGP1 and AtPGP19. Mol Biol Cell. 2003 Oct;14(10):4238-49. Epub 2003 Aug 7. PMID:14517332 doi:http://dx.doi.org/10.1091/mbc.E02-10-0698
↑ Lin R, Wang H. Two homologous ATP-binding cassette transporter proteins, AtMDR1 and AtPGP1, regulate Arabidopsis photomorphogenesis and root development by mediating polar auxin transport. Plant Physiol. 2005 Jun;138(2):949-64. PMID:15908594 doi:10.1104/pp.105.061572
↑ Geisler M, Blakeslee JJ, Bouchard R, Lee OR, Vincenzetti V, Bandyopadhyay A, Titapiwatanakun B, Peer WA, Bailly A, Richards EL, Ejendal KF, Smith AP, Baroux C, Grossniklaus U, Müller A, Hrycyna CA, Dudler R, Murphy AS, Martinoia E. Cellular efflux of auxin catalyzed by the Arabidopsis MDR/PGP transporter AtPGP1. Plant J. 2005 Oct;44(2):179-94. PMID:16212599 doi:10.1111/j.1365-313X.2005.02519.x
↑ Sidler M, Hassa P, Hasan S, Ringli C, Dudler R. Involvement of an ABC transporter in a developmental pathway regulating hypocotyl cell elongation in the light. Plant Cell. 1998 Oct;10(10):1623-36. PMID:9761790 doi:10.1105/tpc.10.10.1623
↑ Wei H, Zhu H, Ying W, Janssens H, Kvasnica M, Winne JM, Gao Y, Friml J, Ma Q, Tan S, Liu X, Russinova E, Sun L. Structural insights into brassinosteroid export mediated by the Arabidopsis ABC transporter ABCB1. Plant Commun. 2025 Jan 13;6(1):101181. PMID:39497419 doi:10.1016/j.xplc.2024.101181

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/8zq4"

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 8zq4 is ON HOLD
+==Structure of the Arabidopsis ABCB1 EQ mutant in the BL plus ATP bound state==
+<StructureSection load='8zq4' size='340' side='right'caption='[[8zq4]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[8zq4]] is a 1 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=8ZQ4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8ZQ4 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.8&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=BLD:BRASSINOLIDE'>BLD</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=8zq4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8zq4 OCA], [https://pdbe.org/8zq4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8zq4 RCSB], [https://www.ebi.ac.uk/pdbsum/8zq4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8zq4 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/AB1B_ARATH AB1B_ARATH] Auxin efflux transporter that acts as a negative regulator of light signaling to promote hypocotyl elongation. Mediates the accumulation of chlorophyll and anthocyanin, as well as the expression of genes in response to light. Participates directly in auxin efflux and thus regulates the polar (presumably basipetal) auxin transport (from root tips to root elongating zone). Transports also some auxin metabolites such as oxindoleacetic acid and indoleacetaldehyde. Involved in diverse auxin-mediated responses including gravitropism, phototropism and lateral root formation. Confers resistance to herbicides such as dicamba, pendimethalin, oryzalin, and monosodium acid methanearsonate (MSMA), but not to herbicides such as glyphosate, atrazine, bentazon and fluazifop-p-butyl. Mediates also resistance to xenobiotics such as cycloheximide and the cytokinin N6-(2-isopentenyl)adenine (2IP).<ref>PMID:10760241</ref> <ref>PMID:11701880</ref> <ref>PMID:12640467</ref> <ref>PMID:14517332</ref> <ref>PMID:15908594</ref> <ref>PMID:16212599</ref> <ref>PMID:9761790</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Brassinosteroids (BRs) are steroidal phytohormones indispensable for plant growth, development, and responses to environmental stresses. The export of bioactive BRs to the apoplast is essential for BR signaling initiation, which requires binding of a BR molecule to the extracellular domains of the plasma membrane-localized receptor complex. We have previously shown that the Arabidopsis thaliana ATP-binding cassette (ABC) transporter ABCB19 functions as a BR exporter and, together with its close homolog ABCB1, positively regulates BR signaling. Here, we demonstrate that ABCB1 is another BR transporter. The ATP hydrolysis activity of ABCB1 can be stimulated by bioactive BRs, and its transport activity was confirmed in proteoliposomes and protoplasts. Structures of ABCB1 were determined in substrate-unbound (apo), brassinolide (BL)-bound, and ATP plus BL-bound states. In the BL-bound structure, BL is bound to the hydrophobic cavity formed by the transmembrane domain and triggers local conformational changes. Together, our data provide additional insights into ABC transporter-mediated BR export.
-Authors:
+Structural insights into brassinosteroid export mediated by the Arabidopsis ABC transporter ABCB1.,Wei H, Zhu H, Ying W, Janssens H, Kvasnica M, Winne JM, Gao Y, Friml J, Ma Q, Tan S, Liu X, Russinova E, Sun L Plant Commun. 2025 Jan 13;6(1):101181. doi: 10.1016/j.xplc.2024.101181. Epub 2024 , Nov 4. PMID:39497419<ref>PMID:39497419</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 8zq4" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Arabidopsis thaliana]]
+[[Category: Large Structures]]
+[[Category: Liu X]]
+[[Category: Sun L]]
+[[Category: Wei H]]
+[[Category: Ying W]]

8zq4

From Proteopedia

Current revision

Structure of the Arabidopsis ABCB1 EQ mutant in the BL plus ATP bound state

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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