EMDB/PDB/SASBDBから引用されている文献のデータベース

キーワード
構造解析手法	All X線回折 NMR 電子顕微鏡小角散乱中性子線回折線維回折粉末回折赤外分光 EPR FRET 理論モデルハイブリッド
著者・登録者
ジャーナル
IF	>30 >20 >10 >5 all

タイトル	Large domain movements through the lipid bilayer mediate substrate release and inhibition of glutamate transporters.
ジャーナル・号・ページ	Elife, Vol. 9, Year 2020
掲載日	2020年11月6日
著者	Xiaoyu Wang / Olga Boudker /
PubMed 要旨	Glutamate transporters are essential players in glutamatergic neurotransmission in the brain, where they maintain extracellular glutamate below cytotoxic levels and allow for rounds of transmission. ...Glutamate transporters are essential players in glutamatergic neurotransmission in the brain, where they maintain extracellular glutamate below cytotoxic levels and allow for rounds of transmission. The structural bases of their function are well established, particularly within a model archaeal homolog, sodium, and aspartate symporter Glt. However, the mechanism of gating on the cytoplasmic side of the membrane remains ambiguous. We report Cryo-EM structures of Glt reconstituted into nanodiscs, including those structurally constrained in the cytoplasm-facing state and either apo, bound to sodium ions only, substrate, or blockers. The structures show that both substrate translocation and release involve movements of the bulky transport domain through the lipid bilayer. They further reveal a novel mode of inhibitor binding and show how solutes release is coupled to protein conformational changes. Finally, we describe how domain movements are associated with the displacement of bound lipids and significant membrane deformations, highlighting the potential regulatory role of the bilayer.
リンク	Elife / PubMed:33155546 / PubMed Central
手法	EM (単粒子)
解像度	3.05 - 3.71 Å
構造データ	21986 6x12 EMDB-21986, PDB-6x12: Inward-facing Apo-open state of the glutamate transporter homologue GltPh 手法: EM (単粒子) / 解像度: 3.52 Å 21987 6x13 EMDB-21987, PDB-6x13: Inward-facing sodium-bound state of the glutamate transporter homologue GltPh 手法: EM (単粒子) / 解像度: 3.66 Å 21988 6x14 EMDB-21988, PDB-6x14: Inward-facing state of the glutamate transporter homologue GltPh in complex with TFB-TBOA 手法: EM (単粒子) / 解像度: 3.71 Å 21989 6x15 EMDB-21989, PDB-6x15: Inward-facing state of the glutamate transporter homologue GltPh in complex with L-aspartate and sodium ions 手法: EM (単粒子) / 解像度: 3.05 Å 21990 6x16 EMDB-21990, PDB-6x16: Inward-facing state of the glutamate transporter homologue GltPh in complex with TBOA 手法: EM (単粒子) / 解像度: 3.39 Å 21991 6x17 EMDB-21991, PDB-6x17: Outward-facing state of the glutamate transporter homologue GltPh in complex with TBOA 手法: EM (単粒子) / 解像度: 3.66 Å
化合物	ChemComp-6OU: [(2~{R})-1-[2-azanylethoxy(oxidanyl)phosphoryl]oxy-3-hexadecanoyloxy-propan-2-yl] (~{Z})-octadec-9-enoate / POPE / リン脂質YM ChemComp-7O9: (2~{S},3~{S})-2-azanyl-3-[[3-[[4-(trifluoromethyl)phenyl]carbonylamino]phenyl]methoxy]butanedioic acid / TFB-TBOA ChemComp-NA: Unknown entry / ナトリウムカチオン ChemComp-ASP: ASPARTIC ACID / アスパラギン酸 ChemComp-HG: Unknown entry ChemComp-HOH: WATER ChemComp-TB1*: (3S)-3-(BENZYLOXY)-L-ASPARTIC ACID / TBOA
由来	pyrococcus horikoshii (古細菌)
キーワード	TRANSPORT PROTEIN / sodium-coupled L-aspartate transporter