3O7P

Crystal structure of the E.coli Fucose:proton symporter, FucP (N162A)

3O7P の概要

• エントリーDOI: 10.2210/pdb3o7p/pdb
• 関連するPDBエントリー: 3O7Q
• 分子名称: L-fucose-proton symporter, nonyl beta-D-glucopyranoside (2 entities in total)
• 機能のキーワード: l-fucose, symporter, multi-pass membrane protein, transporter, transport protein
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cell inner membrane; Multi-pass membrane protein: P11551
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 47837.94

構造登録者

Dang, S.Y.,Sun, L.F.,Wang, J.,Yan, N. (登録日: 2010-07-30, 公開日: 2010-09-15, 最終更新日: 2023-11-01)

主引用文献

Dang, S.Y.,Sun, L.F.,Huang, Y.,Lu, F.,Liu, Y.,Gong, H.,Wang, J.,Yan, N.
Structure of a fucose transporter in an outward-open conformation
Nature, 467:734-738, 2010

PubMed Abstract: The major facilitator superfamily (MFS) transporters are an ancient and widespread family of secondary active transporters. In Escherichia coli, the uptake of l-fucose, a source of carbon for microorganisms, is mediated by an MFS proton symporter, FucP. Despite intensive study of the MFS transporters, atomic structure information is only available on three proteins and the outward-open conformation has yet to be captured. Here we report the crystal structure of FucP at 3.1 Å resolution, which shows that it contains an outward-open, amphipathic cavity. The similarly folded amino and carboxyl domains of FucP have contrasting surface features along the transport path, with negative electrostatic potential on the N domain and hydrophobic surface on the C domain. FucP only contains two acidic residues along the transport path, Asp 46 and Glu 135, which can undergo cycles of protonation and deprotonation. Their essential role in active transport is supported by both in vivo and in vitro experiments. Structure-based biochemical analyses provide insights into energy coupling, substrate recognition and the transport mechanism of FucP.

PubMed: 20877283
DOI: 10.1038/nature09406

実験手法

X-RAY DIFFRACTION (3.196 Å)