4X5N

Crystal structure of SemiSWEET in the inward-open and outward-open conformations

4X5N の概要

• エントリーDOI: 10.2210/pdb4x5n/pdb
• 関連するPDBエントリー: 4X5M
• 分子名称: Uncharacterized protein (1 entity in total)
• 機能のキーワード: sweet, pqlc, membrane protein, sugar transporter, transport protein
• 由来する生物種: Escherichia coli UMEA 3162-1
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 44933.22

構造登録者

Lee, Y.,Nishizawa, T.,Yamashita, K.,Ishitani, R.,Nureki, O. (登録日: 2014-12-05, 公開日: 2015-01-21, 最終更新日: 2023-11-08)

主引用文献

Lee, Y.,Nishizawa, T.,Yamashita, K.,Ishitani, R.,Nureki, O.
Structural basis for the facilitative diffusion mechanism by SemiSWEET transporter
Nat Commun, 6:6112-6112, 2015

PubMed Abstract: SWEET family proteins mediate sugar transport across biological membranes and play crucial roles in plants and animals. The SWEETs and their bacterial homologues, the SemiSWEETs, are related to the PQ-loop family, which is characterized by highly conserved proline and glutamine residues (PQ-loop motif). Although the structures of the bacterial SemiSWEETs were recently reported, the conformational transition and the significance of the conserved motif in the transport cycle have remained elusive. Here we report crystal structures of SemiSWEET from Escherichia coli, in the both inward-open and outward-open states. A structural comparison revealed that SemiSWEET undergoes an intramolecular conformational change in each protomer. The conserved PQ-loop motif serves as a molecular hinge that enables the 'binder clip-like' motion of SemiSWEET. The present work provides the framework for understanding the overall transport cycles of SWEET and PQ-loop family proteins.

PubMed: 25598322
DOI: 10.1038/ncomms7112

実験手法

X-RAY DIFFRACTION (3 Å)