5YS3

1.8 angstrom crystal structure of Succinate-Acetate Permease from Citrobacter koseri

5YS3 の概要

• エントリーDOI: 10.2210/pdb5ys3/pdb
• 分子名称: Succinate-Acetate Permease, ACETATE ION, PALMITIC ACID, ... (5 entities in total)
• 機能のキーワード: organic anion channel, rectifying, unidirectional, dehydration, transport protein
• 由来する生物種: Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 67247.97

構造登録者

Qiu, B.,Liao, J. (登録日: 2017-11-13, 公開日: 2018-04-25, 最終更新日: 2024-03-27)

主引用文献

Qiu, B.,Xia, B.,Zhou, Q.,Lu, Y.,He, M.,Hasegawa, K.,Ma, Z.,Zhang, F.,Gu, L.,Mao, Q.,Wang, F.,Zhao, S.,Gao, Z.,Liao, J.
Succinate-acetate permease from Citrobacter koseri is an anion channel that unidirectionally translocates acetate
Cell Res., 28:644-654, 2018

PubMed Abstract: Acetate is an important metabolite in metabolism and cell signaling. Succinate-Acetate Permease (SatP) superfamily proteins are known to be responsible for acetate transport across membranes, but the nature of this transport remains unknown. Here, we show that the SatP homolog from Citrobacter koseri (SatP_Ck) is an anion channel that can unidirectionally translocate acetate at rates of the order of ~10 ions/s. Crystal structures of SatP_Ck in complex with multiple acetates at 1.8 Å reveal that the acetate pathway consists of four acetate-binding sites aligned in a single file that are interrupted by three hydrophobic constrictions. The bound acetates at the four sites are each orientated differently. The acetate at the cytoplasmic vestibule is partially dehydrated, whereas those in the main pore body are fully dehydrated. Aromatic residues within the substrate pathway may coordinate translocation of acetates via anion-π interactions. SatP_Ck reveals a new type of selective anion channel and provides a structural and functional template for understanding organic anion transport.

PubMed: 29588525
DOI: 10.1038/s41422-018-0032-8

実験手法

X-RAY DIFFRACTION (1.823 Å)