8OMZ

Wide inward-open unliganded UraA in complex with a conformation-selective synthetic nanobody

8OMZ の概要

• エントリーDOI: 10.2210/pdb8omz/pdb
• 分子名称: Uracil permease, Sy45, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (6 entities in total)
• 機能のキーワード: slc23, uracil transporter, uraa, membrane protein, sybody, nanobody
• 由来する生物種: Escherichia coli O157:H7; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 130911.26

構造登録者

Kuhn, B.T.,Geertsma, E.R. (登録日: 2023-03-31, 公開日: 2024-04-10, 最終更新日: 2024-10-23)

主引用文献

Kuhn, B.T.,Zoller, J.,Zimmermann, I.,Gemeinhardt, T.,Ozkul, D.H.,Langer, J.D.,Seeger, M.A.,Geertsma, E.R.
Interdomain-linkers control conformational transitions in the SLC23 elevator transporter UraA.
Nat Commun, 15:7518-7518, 2024

PubMed Abstract: Uptake of nucleobases and ascorbate is an essential process in all living organisms mediated by SLC23 transport proteins. These transmembrane carriers operate via the elevator alternating-access mechanism, and are composed of two rigid domains whose relative motion drives transport. The lack of large conformational changes within these domains suggests that the interdomain-linkers act as flexible tethers. Here, we show that interdomain-linkers are not mere tethers, but have a key regulatory role in dictating the conformational space of the transporter and defining the rotation axis of the mobile transport domain. By resolving a wide inward-open conformation of the SLC23 elevator transporter UraA and combining biochemical studies using a synthetic nanobody as conformational probe with hydrogen-deuterium exchange mass spectrometry, we demonstrate that interdomain-linkers control the function of transport proteins by influencing substrate affinity and transport rate. These findings open the possibility to allosterically modulate the activity of elevator proteins by targeting their linkers.

PubMed: 39209842
DOI: 10.1038/s41467-024-51814-8

実験手法

X-RAY DIFFRACTION (3.5 Å)