1IWM

Crystal Structure of the Outer Membrane Lipoprotein Receptor, LolB

1IWM の概要

• エントリーDOI: 10.2210/pdb1iwm/pdb
• 関連するPDBエントリー: 1IWL 1IWN
• 分子名称: Outer Membrane Lipoprotein LolB, SULFATE ION (3 entities in total)
• 機能のキーワード: unclosed beta barrel, lipoprotein, protein transport
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cell outer membrane; Lipid-anchor: P61320
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 42835.69

構造登録者

Takeda, K.,Miyatake, H.,Yokota, N.,Matsuyama, S.,Tokuda, H.,Miki, K. (登録日: 2002-05-17, 公開日: 2003-07-15, 最終更新日: 2023-12-27)

主引用文献

Takeda, K.,Miyatake, H.,Yokota, N.,Matsuyama, S.,Tokuda, H.,Miki, K.
Crystal structures of bacterial lipoprotein localization factors, LolA and LolB.
Embo J., 22:3199-3209, 2003

PubMed Abstract: Lipoproteins having a lipid-modified cysteine at the N-terminus are localized on either the inner or the outer membrane of Escherichia coli depending on the residue at position 2. Five Lol proteins involved in the sorting and membrane localization of lipoprotein are highly conserved in Gram-negative bacteria. We determined the crystal structures of a periplasmic chaperone, LolA, and an outer membrane lipoprotein receptor, LolB. Despite their dissimilar amino acid sequences, the structures of LolA and LolB are strikingly similar to each other. Both have a hydrophobic cavity consisting of an unclosed beta barrel and an alpha-helical lid. The cavity represents a possible binding site for the lipid moiety of lipoproteins. Detailed structural differences between the two proteins provide significant insights into the molecular mechanisms underlying the energy-independent transfer of lipoproteins from LolA to LolB and from LolB to the outer membrane. Furthermore, the structures of both LolA and LolB determined from different crystal forms revealed the distinct structural dynamics regarding the association and dissociation of lipoproteins. The results are discussed in the context of the current model for the lipoprotein transfer from the inner to the outer membrane through a hydrophilic environment.

PubMed: 12839983
DOI: 10.1093/emboj/cdg324

実験手法

X-RAY DIFFRACTION (1.9 Å)