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	Narrowed pore conformations of aquaglyceroporins AQP3 and GlpF.
ジャーナル・号・ページ	Nat Commun, Vol. 16, Issue 1, Page 2653, Year 2025
掲載日	2025年3月20日
著者	Daisuke Kozai / Masao Inoue / Shota Suzuki / Akiko Kamegawa / Kouki Nishikawa / Hiroshi Suzuki / Toru Ekimoto / Mitsunori Ikeguchi / Yoshinori Fujiyoshi /
PubMed 要旨	Aquaglyceroporins such as aquaporin-3 (AQP3) and its bacterial homologue GlpF facilitate water and glycerol permeation across lipid bilayers. X-ray crystal structures of GlpF showed open pore ...Aquaglyceroporins such as aquaporin-3 (AQP3) and its bacterial homologue GlpF facilitate water and glycerol permeation across lipid bilayers. X-ray crystal structures of GlpF showed open pore conformations, and AQP3 has also been predicted to adopt this conformation. Here we present cryo-electron microscopy structures of rat AQP3 and GlpF in different narrowed pore conformations. In n-dodecyl-β-D-maltopyranoside detergent micelles, aromatic/arginine constriction filter residues of AQP3 containing Tyr212 form a 2.8-Å diameter pore, whereas in 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC) nanodiscs, Tyr212 inserts into the pore. Molecular dynamics simulation shows the Tyr212-in conformation is stable and largely suppresses water permeability. AQP3 reconstituted in POPC liposomes exhibits water and glycerol permeability, suggesting that the Tyr212-in conformation may be altered during permeation. AQP3 Y212F and Y212T mutant structures suggest that the aromatic residue drives the pore-inserted conformation. The aromatic residue is conserved in AQP7 and GlpF, but neither structure exhibits the AQP3-like conformation in POPC nanodiscs. Unexpectedly, the GlpF pore is covered by an intracellular loop, but the loop is flexible and not primarily related to the GlpF permeability. Our findings illuminate the unique AQP3 conformation and structural diversity of aquaglyceroporins.
リンク	Nat Commun / PubMed:40113770 / PubMed Central
手法	EM (単粒子)
解像度	2.26 - 3.74 Å
構造データ	39052 8y8n EMDB-39052, PDB-8y8n: Cryo-EM structure of AQP3 in DDM micelle 手法: EM (単粒子) / 解像度: 3.12 Å 39053 8y8o EMDB-39053, PDB-8y8o: Cryo-EM structure of AQP3 in POPC nanodisc 手法: EM (単粒子) / 解像度: 2.94 Å 39054 8y8p EMDB-39054, PDB-8y8p: Cryo-EM structure of AQP3 Y212F in POPC nanodisc 手法: EM (単粒子) / 解像度: 2.9 Å 39055 8y8q EMDB-39055, PDB-8y8q: Cryo-EM structure of AQP3 Y212T in POPC nanodisc 手法: EM (単粒子) / 解像度: 2.67 Å 39056 8y8r EMDB-39056, PDB-8y8r: Cryo-EM structure of AQP3 Y212T in DDM micelle 手法: EM (単粒子) / 解像度: 3.39 Å 39057 8y8s EMDB-39057, PDB-8y8s: Cryo-EM structure of AQP3 in DMPC nanodisc 手法: EM (単粒子) / 解像度: 3.03 Å 39060 8y8v EMDB-39060, PDB-8y8v: Cryo-EM structure of AQP7 in POPC nanodisc 手法: EM (単粒子) / 解像度: 2.49 Å EMDB-39061: Cryo-EM map of GlpF in DDM micelle 手法: EM (単粒子) / 解像度: 3.74 Å 39062 8y8w EMDB-39062, PDB-8y8w: Cryo-EM structure of GlpF in POPC nanodisc 手法: EM (単粒子) / 解像度: 2.43 Å 39063 8y8x EMDB-39063, PDB-8y8x: Cryo-EM structure of GlpF with P177 deletion in POPC nanodisc 手法: EM (単粒子) / 解像度: 2.26 Å
化合物	ChemComp-LMT: DODECYL-BETA-D-MALTOSIDE / ドデシルβ-D-マルトシド / 可溶化剤YM ChemComp-P5S*: O-[(R)-{[(2R)-2,3-bis(octadecanoyloxy)propyl]oxy}(hydroxy)phosphoryl]-L-serine / O-(1-O,2-O-ジステアロイル-L-グリセロ-3-ホスホ)セリン
由来	rattus norvegicus (ドブネズミ) homo sapiens (ヒト) escherichia coli (大腸菌) aequorea victoria (オワンクラゲ)
キーワード	MEMBRANE PROTEIN / water channel / aquaporin / aquaglyceroporin / glycerol