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	The role of membrane destabilisation and protein dynamics in BAM catalysed OMP folding.
ジャーナル・号・ページ	Nat Commun, Vol. 12, Issue 1, Page 4174, Year 2021
掲載日	2021年7月7日
著者	Paul White / Samuel F Haysom / Matthew G Iadanza / Anna J Higgins / Jonathan M Machin / James M Whitehouse / Jim E Horne / Bob Schiffrin / Charlotte Carpenter-Platt / Antonio N Calabrese / Kelly M Storek / Steven T Rutherford / David J Brockwell / Neil A Ranson / Sheena E Radford /
PubMed 要旨	The folding of β-barrel outer membrane proteins (OMPs) in Gram-negative bacteria is catalysed by the β-barrel assembly machinery (BAM). How lateral opening in the β-barrel of the major subunit ...The folding of β-barrel outer membrane proteins (OMPs) in Gram-negative bacteria is catalysed by the β-barrel assembly machinery (BAM). How lateral opening in the β-barrel of the major subunit BamA assists in OMP folding, and the contribution of membrane disruption to BAM catalysis remain unresolved. Here, we use an anti-BamA monoclonal antibody fragment (Fab1) and two disulphide-crosslinked BAM variants (lid-locked (LL), and POTRA-5-locked (P5L)) to dissect these roles. Despite being lethal in vivo, we show that all complexes catalyse folding in vitro, albeit less efficiently than wild-type BAM. CryoEM reveals that while Fab1 and BAM-P5L trap an open-barrel state, BAM-LL contains a mixture of closed and contorted, partially-open structures. Finally, all three complexes globally destabilise the lipid bilayer, while BamA does not, revealing that the BAM lipoproteins are required for this function. Together the results provide insights into the role of BAM structure and lipid dynamics in OMP folding.
リンク	Nat Commun / PubMed:34234105 / PubMed Central
手法	EM (単粒子) / X線回折
解像度	2.95 - 10.3 Å
構造データ	12232 7bnq EMDB-12232, PDB-7bnq: Lateral-closed conformation of the lid-locked BAM complex (BamA E435C S665C, BamBDCE) by cryoEM 手法: EM (単粒子) / 解像度: 4.1 Å 12262 7nbx EMDB-12262, PDB-7nbx: Lateral-open conformation of the lid-locked BAM complex (BamA E435C S665C, BamBDCE) by cryoEM 手法: EM (単粒子) / 解像度: 4.8 Å EMDB-12263: structure of a POTRA-locked BAM complex in a lateral-open conformation 手法: EM (単粒子) / 解像度: 10.3 Å 12271 7ncs EMDB-12271, PDB-7ncs: Lateral-open conformation of the lid-locked BAM complex (BamA E435C S665C, BamBDCE) bound by a bactericidal Fab fragment 手法: EM (単粒子) / 解像度: 7.1 Å 12272 7nd0 EMDB-12272, PDB-7nd0: lateral-open conformation of the wild-type BAM complex (BamABCDE) bound to a bactericidal Fab fragment 手法: EM (単粒子) / 解像度: 5.2 Å PDB-7bm5: Crystal structure of Fab1, the Fab fragment of the anti-BamA monoclonal antibody MAB1 手法: X-RAY DIFFRACTION / 解像度: 2.95 Å
由来	escherichia coli (strain k12) (大腸菌) escherichia coli k-12 (大腸菌) homo sapiens (ヒト) Escherichia coli K-12
キーワード	IMMUNE SYSTEM / Antibody / antibiotic / Fab / BamA / MEMBRANE PROTEIN / Outer membrane protein assembly / beta-barrel / Gram negative bacteria / protein foldase