3SNS

Crystal structure of the C-terminal domain of Escherichia coli lipoprotein BamC

3SNS の概要

• エントリーDOI: 10.2210/pdb3sns/pdb
• 関連するPDBエントリー: 2LAF 2YH5
• 分子名称: Lipoprotein 34, CHLORIDE ION (3 entities in total)
• 機能のキーワード: alpha/beta, bacterial outer membrane protein assembly, bam complex proteins, e. coli outer membrane, lipid anchored outer membrane protein, protein transport
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cell outer membrane; Lipid-anchor: P0A903
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12927.18

構造登録者

Kim, K.H.,Aulakh, S.,Tan, W.,Paetzel, M. (登録日: 2011-06-29, 公開日: 2011-08-24, 最終更新日: 2023-09-13)

主引用文献

Kim, K.H.,Aulakh, S.,Tan, W.,Paetzel, M.
Crystallographic analysis of the C-terminal domain of the Escherichia coli lipoprotein BamC.
Acta Crystallogr.,Sect.F, 67:1350-1358, 2011

PubMed Abstract: In Gram-negative bacteria, the BAM complex catalyzes the essential process of assembling outer membrane proteins. The BAM complex in Escherichia coli consists of five proteins: one β-barrel membrane protein, BamA, and four lipoproteins, BamB, BamC, BamD and BamE. Here, the crystal structure of the C-terminal domain of E. coli BamC (BamC(C): Ala224-Ser343) refined to 1.5 Å resolution in space group H3 is reported. BamC(C) consists of a six-stranded antiparallel β-sheet, three α-helices and one 3(10)-helix. Sequence and surface analysis reveals that most of the conserved residues within BamC(C) are localized to form a continuous negatively charged groove that is involved in a major crystalline lattice contact in which a helix from a neighbouring BamC(C) binds against this surface. This interaction is topologically and architecturally similar to those seen in the substrate-binding grooves of other proteins with BamC-like folds. Taken together, these results suggest that an identified surface on the C-terminal domain of BamC may serve as an important protein-binding surface for interaction with other BAM-complex components or substrates.

PubMed: 22102230
DOI: 10.1107/S174430911103363X

実験手法

X-RAY DIFFRACTION (1.5 Å)