3KBC

Crystal structure of GltPh K55C-A364C mutant crosslinked with divalent mercury

3KBC の概要

• エントリーDOI: 10.2210/pdb3kbc/pdb
• 関連するPDBエントリー: 1XFH 2NWL 2NWW 2NWX
• 分子名称: 425aa long hypothetical proton glutamate symport protein, ASPARTIC ACID, MERCURY (II) ION, ... (4 entities in total)
• 機能のキーワード: amino acid transporter, transmembrane transporter, aspartate transporter, transport protein, cysteine cross-link, inward-facing
• 由来する生物種: Pyrococcus horikoshii
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 135806.59

構造登録者

Reyes, N.,Ginter, C.,Boudker, O. (登録日: 2009-10-20, 公開日: 2009-12-01, 最終更新日: 2023-09-06)

主引用文献

Reyes, N.,Ginter, C.,Boudker, O.
Transport mechanism of a bacterial homologue of glutamate transporters.
Nature, 462:880-885, 2009

PubMed Abstract: Glutamate transporters are integral membrane proteins that catalyse a thermodynamically uphill uptake of the neurotransmitter glutamate from the synaptic cleft into the cytoplasm of glia and neuronal cells by harnessing the energy of pre-existing electrochemical gradients of ions. Crucial to the reaction is the conformational transition of the transporters between outward and inward facing states, in which the substrate binding sites are accessible from the extracellular space and the cytoplasm, respectively. Here we describe the crystal structure of a double cysteine mutant of a glutamate transporter homologue from Pyrococcus horikoshii, Glt(Ph), which is trapped in the inward facing state by cysteine crosslinking. Together with the previously determined crystal structures of Glt(Ph) in the outward facing state, the structure of the crosslinked mutant allows us to propose a molecular mechanism by which Glt(Ph) and, by analogy, mammalian glutamate transporters mediate sodium-coupled substrate uptake.

PubMed: 19924125
DOI: 10.1038/nature08616

実験手法

X-RAY DIFFRACTION (3.51 Å)