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	Conformational plasticity across phylogenetic clusters of RND multidrug efflux pumps and its impact on substrate specificity.
ジャーナル・号・ページ	Nat Commun, Vol. 16, Issue 1, Page 11649, Year 2025
掲載日	2025年11月26日
著者	Mariya Lazarova / Thomas Eicher / Clara Börnsen / Hui Zeng / Mohd Athar / Ui Okada / Eiki Yamashita / Inga M Spannaus / Max Borgosch / Hi-Jea Cha / Attilio V Vargiu / Satoshi Murakami / Kay Diederichs / Achilleas S Frangakis / Klaas M Pos /
PubMed 要旨	Antibiotic efflux plays a key role for the multidrug resistance in Gram-negative bacteria. Multidrug efflux pumps of the resistance nodulation and cell division (RND) superfamily function as part of ...Antibiotic efflux plays a key role for the multidrug resistance in Gram-negative bacteria. Multidrug efflux pumps of the resistance nodulation and cell division (RND) superfamily function as part of cell envelope spanning systems and provide resistance to diverse antibiotics. Here, we identify two phylogenetic clusters of RND proteins with conserved binding pocket residues and show that the transfer of a single conserved residue between both clusters affects the resistance phenotype not only due to changes in the physicochemical properties of the binding pocket, but also due to an altered equilibrium between the conformational states of the transport cycle. We demonstrate, using single-particle cryo-electron microscopy, that AcrB and OqxB, which represent both clusters, adopt fundamentally different apo states, implying distinct mechanisms for initial substrate binding. The observed conformational plasticity appears phylogenetically conserved and likely plays a role in the diversification of the resistance phenotype among homologous RND pumps.
リンク	Nat Commun / PubMed:41298458 / PubMed Central
手法	EM (単粒子) / X線回折
解像度	1.89 - 3.9 Å
構造データ	EMDB-50328: Single particle cryo-EM maps of AcrB wildtype monomer classes in DDM 手法: EM (単粒子) / 解像度: 3.6 Å EMDB-50329: Single particle cryo-EM maps of AcrB V612F monomer classes in DDM 手法: EM (単粒子) / 解像度: 3.9 Å 50331 9fdp EMDB-50331: Single particle cryo-EM maps of AcrB V612W monomer classes in DDM PDB-9fdp: Single particle cryo-EM structure of the AcrB V612W monomer in the O state 手法: EM (単粒子) / 解像度: 3.3 Å 50332 9fdq EMDB-50332: Single particle cryo-EM maps of AcrB V612F monomer classes in salipro nanodiscs PDB-9fdq: Single particle cryo-EM structure of the AcrB V612F monomer in the O state 手法: EM (単粒子) / 解像度: 3.47 Å 50334 9fdz EMDB-50334, PDB-9fdz: Single particle cryo-EM structure of the multidrug efflux pump OqxB from Klebsiella pneumoniae 手法: EM (単粒子) / 解像度: 2.86 Å EMDB-50335: Single particle cryo-EM maps of OqxB monomer classes in salipro nanodiscs 手法: EM (単粒子) / 解像度: 3.59 Å EMDB-50645: Single particle cryo-EM maps of AcrB wildtype monomers reconstituted in salipro nanodiscs 手法: EM (単粒子) / 解像度: 2.9 Å PDB-8zxs: Crystal structure of multidrug efflux transporter OqxB from Klebsiella pneumoniae 手法: X-RAY DIFFRACTION / 解像度: 2.75 Å PDB-9fe2: Crystallographic structure of AcrB V612W with bound minocycline 手法: X-RAY DIFFRACTION / 解像度: 1.89 Å PDB-9fe3: Crystallographic structure of AcrB V612W 手法: X-RAY DIFFRACTION / 解像度: 2.3 Å PDB-9fe4: Crystallographic structure of AcrB V612F 手法: X-RAY DIFFRACTION / 解像度: 2.8 Å PDB-9fhc: Crystallographic structure of AcrB V612F with bound minocycline 手法: X-RAY DIFFRACTION / 解像度: 2.2 Å PDB-9fhg: Crystallographic structure of AcrB V612N in LTO state 手法: X-RAY DIFFRACTION / 解像度: 3 Å PDB-9fhj: Crystallographic structure of AcrB V612N in TTT state 手法: X-RAY DIFFRACTION / 解像度: 3.55 Å
化合物	ChemComp-LMT: DODECYL-BETA-D-MALTOSIDE / 可溶化剤YM ChemComp-GOL: GLYCEROL ChemComp-HOH: WATER ChemComp-MIY: (4S,4AS,5AR,12AS)-4,7-BIS(DIMETHYLAMINO)-3,10,12,12A-TETRAHYDROXY-1,11-DIOXO-1,4,4A,5,5A,6,11,12A-OCTAHYDROTETRACENE-2- / 薬剤, 抗生剤YM
由来	escherichia coli k-12 (大腸菌) klebsiella pneumoniae (肺炎桿菌) synthetic construct (人工物)
キーワード	MEMBRANE PROTEIN / Multidrug efflux transporter / Membrane transporter / Antimicrobial resistance / AMR / Klebsiella pneumoniae / TRANSPORT PROTEIN / Drug efflux / RND transporter