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	Rhodamine6G and Hœchst33342 narrow BmrA conformational spectrum for a more efficient use of ATP.
ジャーナル・号・ページ	Nat Commun, Vol. 16, Issue 1, Page 1745, Year 2025
掲載日	2025年2月18日
著者	A Gobet / L Moissonnier / E Zarkadas / S Magnard / E Bettler / J Martin / R Terreux / G Schoehn / C Orelle / J M Jault / P Falson / V Chaptal /
PubMed 要旨	Multidrug ABC transporters harness the energy of ATP binding and hydrolysis to translocate substrates out of the cell and detoxify them. While this involves a well-accepted alternating access ...Multidrug ABC transporters harness the energy of ATP binding and hydrolysis to translocate substrates out of the cell and detoxify them. While this involves a well-accepted alternating access mechanism, molecular details of this interplay are still elusive. Rhodamine6G binding on a catalytic inactive mutant of the homodimeric multidrug ABC transporter BmrA triggers a cooperative binding of ATP on the two identical nucleotide-binding-sites, otherwise michaelian. Here, we investigate this asymmetric behavior via a structural-enzymology approach, solving cryoEM structures of BmrA at defined ATP ratios, highlighting the plasticity of BmrA as it undergoes the transition from inward to outward facing conformations. Analysis of continuous heterogeneity within cryoEM data and structural dynamics, reveals that Rhodamine6G narrows the conformational spectrum explored by the nucleotide-binding domains. We observe the same behavior for the other drug Hœchst33342. Following on these findings, the effect of drug-binding showed an ATPase stimulation and a maximal transport activity of the wild-type protein at the concentration-range where the cooperative transition occurs. Altogether, these findings provide a description of the influence of drug binding on the ATP-binding sites through a change in conformational dynamics.
リンク	Nat Commun / PubMed:39966360 / PubMed Central
手法	EM (単粒子)
解像度	3.3 - 4.4 Å
構造データ	19113 8rez EMDB-19113, PDB-8rez: BmrA E504-apo 手法: EM (単粒子) / 解像度: 3.3 Å 19115 8rf1 EMDB-19115, PDB-8rf1: BmrA E504-R6G 手法: EM (単粒子) / 解像度: 4.3 Å 19130 8rg7 EMDB-19130, PDB-8rg7: BmrA E504-R6G-25uMATP-Mg 手法: EM (単粒子) / 解像度: 3.9 Å 19131 8rga EMDB-19131, PDB-8rga: BmrA E504-25uMATPMg 手法: EM (単粒子) / 解像度: 3.7 Å 19135 8rgn EMDB-19135, PDB-8rgn: BmrA E504-R6G-70uMATPMg 手法: EM (単粒子) / 解像度: 3.7 Å 19180 8ri1 EMDB-19180, PDB-8ri1: BmrA E504-100uMATPMg 手法: EM (単粒子) / 解像度: 3.6 Å 19185 8ria EMDB-19185, PDB-8ria: BmrA E504-100uMATPMg-IF 手法: EM (単粒子) / 解像度: 4.4 Å 51550 9gsj EMDB-51550, PDB-9gsj: BmrA E504A in complex with Hoechst33342 手法: EM (単粒子) / 解像度: 3.6 Å
化合物	ChemComp-RHQ: RHODAMINE 6G ChemComp-ATP: ADENOSINE-5'-TRIPHOSPHATE / ATP / ATP, エネルギー貯蔵分子YM ChemComp-MG: Unknown entry / マグネシウムジカチオン ChemComp-HOH: WATER ChemComp-HT1*: 2'-(4-ETHOXYPHENYL)-5-(4-METHYL-1-PIPERAZINYL)-2,5'-BI-BENZIMIDAZOLE / Hoechst-33342
由来	bacillus subtilis (枯草菌)
キーワード	TRANSPORT PROTEIN / BmrA / multidrug transporter / drug resistance / ABC transporter / MEMBRANE PROTEIN / transporter complex with Hoechst33342