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	Liganded LolCDE structures reveal a common substrate-LolE interaction guiding bacterial lipoprotein transport.
ジャーナル・号・ページ	Proc Natl Acad Sci U S A, Vol. 123, Issue 4, Page e2520579123, Year 2026
掲載日	2026年1月27日
著者	Paul Szewczyk / Nicholas P Greene / Martyn F Symmons / Steven W Hardwick / Vassilis Koronakis /
PubMed 要旨	Bacterial lipoproteins are key structural components of the outer membrane in Gram-negative bacteria and vital components of machineries required for its biosynthesis and maintenance. The Lol system, ...Bacterial lipoproteins are key structural components of the outer membrane in Gram-negative bacteria and vital components of machineries required for its biosynthesis and maintenance. The Lol system, essential for viability, directs transport of lipoproteins from the site of biosynthesis on the inner membrane to the outer membrane and has been the target of extensive efforts to develop novel antimicrobial drugs. In the first stage of this transport process, newly synthesized lipoproteins are released from the inner membrane by the ABC transporter LolCDE and passed to the periplasmic chaperone, LolA. Here, we show cryo-EM structures of LolCDE in complex with three different lipoprotein substrates, Lpp, Pal, and LolB, with the latter two bearing a disordered peptide linker between the acyl chains and the globular domain. Our work reveals that when the mature lipoprotein lacks an unstructured linker, the N-terminal portion of the protein is in an unfolded state for transport. The lipoproteins make a sequence-independent but structurally conserved interaction with a cleft on the surface of the periplasmic domain of LolE that promotes efficient transport. We propose a model of lipoprotein export where this interaction acts as pivot point for the peptide portion of the lipoprotein allowing the acyl chains to rotate 180° from their initial position in LolCDE to their binding site in LolA. Our results demonstrate how LolCDE can extrude lipoproteins of diverse sequence and structure and reveal an important detail of a transport process fundamental to bacterial physiology.
リンク	Proc Natl Acad Sci U S A / PubMed:41557797 / PubMed Central
手法	EM (単粒子)
解像度	2.8 - 3.63 Å
構造データ	54033 9rlc EMDB-54033, PDB-9rlc: LolCDE complex with Lpp lipoprotein 手法: EM (単粒子) / 解像度: 2.8 Å 54034 9rld EMDB-54034, PDB-9rld: LolCDE complex with Lpp lipoprotein 手法: EM (単粒子) / 解像度: 3.0 Å 54035 9rle EMDB-54035, PDB-9rle: LolCDE complex with Pal lipoprotein 手法: EM (単粒子) / 解像度: 3.18 Å 54036 9rlf EMDB-54036, PDB-9rlf: LolCDE complex with Pal lipoprotein 手法: EM (単粒子) / 解像度: 3.17 Å 54037 9rlg EMDB-54037, PDB-9rlg: LolCDE complex with LolB lipoprotein 手法: EM (単粒子) / 解像度: 3.09 Å 54038 9rlh EMDB-54038, PDB-9rlh: LolCDE complex with del 9-15 LolB lipoprotein 手法: EM (単粒子) / 解像度: 3.19 Å 54039 9rli EMDB-54039, PDB-9rli: LolCDEdelta(235-252) complex with Pal lipoprotein 手法: EM (単粒子) / 解像度: 3.63 Å 54040 9rlj EMDB-54040, PDB-9rlj: LolCDE with bound ATPgammaS 手法: EM (単粒子) / 解像度: 2.9 Å 54041 9rlk EMDB-54041, PDB-9rlk: LolCDE(delta 235-252) complex with Pal lipoprotein 手法: EM (単粒子) / 解像度: 3.29 Å EMDB-54478: LolCDE LolE R239C Y250C mutant closed conformation 手法: EM (単粒子) / 解像度: 3.26 Å EMDB-54479: LolCDE LolE R239C Y250 mutant open conformation 手法: EM (単粒子) / 解像度: 3.48 Å
化合物	ChemComp-PLM: PALMITIC ACID ChemComp-Z41: (2S)-3-hydroxypropane-1,2-diyl dihexadecanoate ChemComp-AGS: PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER / ATP-gamma-S, エネルギー貯蔵分子類似体YM ChemComp-MG*: Unknown entry
由来	Escherichia coli (大腸菌) escherichia coli k-12 (大腸菌)
キーワード	PROTEIN TRANSPORT / Gram-negative / envelope biogenesis / outer membrane protein