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	Stepwise ATP translocation into the endoplasmic reticulum by human SLC35B1.
ジャーナル・号・ページ	Nature, Vol. 643, Issue 8072, Page 855-864, Year 2025
掲載日	2025年5月21日
著者	Ashutosh Gulati / Do-Hwan Ahn / Albert Suades / Yurie Hult / Gernot Wolf / So Iwata / Giulio Superti-Furga / Norimichi Nomura / David Drew /
PubMed 要旨	ATP generated in the mitochondria is exported by an ADP/ATP carrier of the SLC25 family. The endoplasmic reticulum (ER) cannot synthesize ATP but must import cytoplasmic ATP to energize protein ...ATP generated in the mitochondria is exported by an ADP/ATP carrier of the SLC25 family. The endoplasmic reticulum (ER) cannot synthesize ATP but must import cytoplasmic ATP to energize protein folding, quality control and trafficking. It was recently proposed that a member of the nucleotide sugar transporter family, termed SLC35B1 (also known as AXER), is not a nucleotide sugar transporter but a long-sought-after ER importer of ATP. Here we report that human SLC35B1 does not bind nucleotide sugars but indeed executes strict ATP/ADP exchange with uptake kinetics consistent with the import of ATP into crude ER microsomes. A CRISPR-Cas9 cell-line knockout demonstrated that SLC35B1 clusters with the most essential SLC transporters for cell growth, consistent with its proposed physiological function. We have further determined seven cryogenic electron microscopy structures of human SLC35B1 in complex with an Fv fragment and either bound to an ATP analogue or ADP in all major conformations of the transport cycle. We observed that nucleotides were vertically repositioned up to approximately 6.5 Å during translocation while retaining key interactions with a flexible substrate-binding site. We conclude that SLC35B1 operates by a stepwise ATP translocation mechanism, which is a previously undescribed model for substrate translocation by an SLC transporter.
リンク	Nature / PubMed:40399679 / PubMed Central
手法	EM (単粒子)
解像度	2.85 - 3.4 Å
構造データ	51528 9gry EMDB-51528, PDB-9gry: Cryo-EM structure of human SLC35B1-Q113F variant with AMP-PNP 手法: EM (単粒子) / 解像度: 3.0 Å 51529 9grz EMDB-51529, PDB-9grz: Cryo-EM structure of human SLC35B1 with AMP-PNP 手法: EM (単粒子) / 解像度: 3.4 Å 51538 9gs3 EMDB-51538, PDB-9gs3: Cryo-EM structure of human SLC35B1-E33A variant with ADP in inward facing conformation 手法: EM (単粒子) / 解像度: 3.15 Å 51539 9gs5 EMDB-51539, PDB-9gs5: Cryo-EM structure of human SLC35B1-E33A variant with ADP in outward facing conformation 手法: EM (単粒子) / 解像度: 3.1 Å 51541 9gs7 EMDB-51541, PDB-9gs7: Cryo-EM structure of human SLC35B1-E33A variant with AMP-PNP 手法: EM (単粒子) / 解像度: 3.15 Å 51551 9gsl EMDB-51551, PDB-9gsl: Cryo-EM structure of human SLC35B1 in inward facing conformation 手法: EM (単粒子) / 解像度: 3.37 Å 52578 9i20 EMDB-52578, PDB-9i20: Cryo-EM structure of human SLC35B1 with ADP 手法: EM (単粒子) / 解像度: 2.85 Å
化合物	ChemComp-ANP: PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / AMP-PNP, エネルギー貯蔵分子類似体YM ChemComp-ADP: ADENOSINE-5'-DIPHOSPHATE / ADP, エネルギー貯蔵分子YM ChemComp-PEV: (1S)-2-{[(2-AMINOETHOXY)(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL STEARATE / POPE, リン脂質*YM
由来	homo sapiens (ヒト) mus musculus (ハツカネズミ)
キーワード	TRANSPORT PROTEIN / ATP:ADP exchanger / AXER / AMP-PNP / membrane protein / ER membrane protein / ADP