We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

9utd

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (05:28, 24 December 2025) (edit) (undo)
 
Line 1: Line 1:
-
'''Unreleased structure'''
 
-
The entry 9utd is ON HOLD until Paper Publication
+
==influx carrier substrate bound form==
 +
<StructureSection load='9utd' size='340' side='right'caption='[[9utd]], [[Resolution|resolution]] 3.06&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[9utd]] 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=9UTD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9UTD 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]] 3.06&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CFA:(2,4-DICHLOROPHENOXY)ACETIC+ACID'>CFA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=9utd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9utd OCA], [https://pdbe.org/9utd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9utd RCSB], [https://www.ebi.ac.uk/pdbsum/9utd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9utd ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/AUX1_ARATH AUX1_ARATH] Carrier protein involved in proton-driven auxin influx. Mediates the formation of auxin gradient from developing leaves (site of auxin biosynthesis) to tips by contributing to the loading of auxin in vascular tissues and facilitating acropetal (base to tip) auxin transport within inner tissues of the root apex, and basipetal (tip to base) auxin transport within outer tissues of the root apex. Unloads auxin from the mature phloem to deliver the hormone to the root meristem via the protophloem cell files. Coordinated subcellular localization of AUX1 is regulated by a brefeldin A-sensitive (BFA) vesicle trafficking process. Involved in lateral root formation, trichoblast polarization and root hair elongation. Required for gravitropism and thigmotropism, especially in roots, by modulating responses to auxin, ethylene and cytokinins such as benzyladenine (BA). Needed for ammonium-mediated root-growth inhibition. Confers sensitivity to the herbicide 2,4-dichlorophenoxyacetic acid (2,4-D, auxin analog), and to polar auxin transport inhibitors such as N-1-naphthylphthalamic acid (NPA) and 2,3,5-triiodobenzoic acid (TIBA).<ref>PMID:10036773</ref> <ref>PMID:10205161</ref> <ref>PMID:11260496</ref> <ref>PMID:11266581</ref> <ref>PMID:11536712</ref> <ref>PMID:11641271</ref> <ref>PMID:11864575</ref> <ref>PMID:11910006</ref> <ref>PMID:12481073</ref> <ref>PMID:15486104</ref> <ref>PMID:16667854</ref> <ref>PMID:7768447</ref> <ref>PMID:8278539</ref> <ref>PMID:8688077</ref> <ref>PMID:9032965</ref> <ref>PMID:9484486</ref> <ref>PMID:9697346</ref> <ref>PMID:11864575</ref> <ref>PMID:9032965</ref> <ref>PMID:11260496</ref> <ref>PMID:11536712</ref>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Auxin regulates numerous aspects of plant growth and development, featuring polar auxin transport mediated by auxin efflux and influx carriers. AUX1 is the major auxin importer that actively takes up natural and synthetic auxins. However, the precise mechanisms underlying AUX1-mediated auxin recognition and transport remain elusive. Here, we present cryoelectron microscopy structures of Arabidopsis thaliana AUX1 in both apo and auxin-bound states, revealing the structural basis for auxin recognition. Structural analyses show that AUX1 assumes the LeuT-like fold in an inward-facing conformation and the auxin analog 2,4-D is recognized by polar residues located in the central cavity of AUX1. Furthermore, we identify a putative cation-binding site that contributes to stabilizing the inward-facing conformation. Interestingly, we reveal that His249 undergoes a substantial conformational shift, and its mutation completely abolishes transport activity, suggesting a crucial role for His249 in AUX1 gating. Collectively, this study provides a structural foundation for a deeper understanding of auxin influx by AUX1-like carriers.
-
Authors:
+
Structural basis of auxin recognition and transport by the plant influx carrier AUX1.,Chen H, Fan J, Chi C, Zhao J, Wu D, Lei X, Deng XW, Jiang D Mol Plant. 2025 Aug 4;18(8):1284-1293. doi: 10.1016/j.molp.2025.06.015. Epub 2025 , Jun 26. PMID:40579814<ref>PMID:40579814</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 9utd" style="background-color:#fffaf0;"></div>
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Arabidopsis thaliana]]
 +
[[Category: Large Structures]]
 +
[[Category: Chen H]]
 +
[[Category: Jiang D]]

Current revision

influx carrier substrate bound form

PDB ID 9utd

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/9utd"
Personal tools