2YH9

Crystal structure of the dimeric BamE from E. coli

2YH9 の概要

• エントリーDOI: 10.2210/pdb2yh9/pdb
• 分子名称: SMALL PROTEIN A (2 entities in total)
• 機能のキーワード: lipoprotein, 3d domain swap, membrane protein
• 由来する生物種: ESCHERICHIA COLI
• 細胞内の位置: Cell outer membrane; Lipid-anchor (By similarity): P0A937
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 29722.84

構造登録者

Zeth, K.,Albrecht, R. (登録日: 2011-04-27, 公開日: 2011-06-29, 最終更新日: 2024-10-23)

主引用文献

Albrecht, R.,Zeth, K.
Structural Basis of Outer Membrane Protein Biogenesis in Bacteria.
J.Biol.Chem., 286:27792-, 2011

PubMed Abstract: In Escherichia coli, a multicomponent BAM (β-barrel assembly machinery) complex is responsible for recognition and assembly of outer membrane β-barrel proteins. The functionality of BAM in protein biogenesis is mainly orchestrated through the presence of two essential components, BamA and BamD. Here, we present crystal structures of four lipoproteins (BamB-E). Monomeric BamB and BamD proteins display scaffold architectures typically implied in transient protein interactions. BamB is a β-propeller protein comprising eight WD40 repeats. BamD shows an elongated fold on the basis of five tetratricopeptide repeats, three of which form the scaffold for protein recognition. The rod-shaped BamC protein has evolved through the gene duplication of two conserved domains known to mediate protein interactions in structurally related complexes. By contrast, the dimeric BamE is formed through a domain swap and indicates fold similarity to the β-lactamase inhibitor protein family, possibly integrating cell wall stability in BAM function. Structural and biochemical data show evidence for the specific recognition of amphipathic sequences through the tetratricopeptide repeat architecture of BamD. Collectively, our data advance the understanding of the BAM complex and highlight the functional importance of BamD in amphipathic outer membrane β-barrel protein motif recognition and protein delivery.

PubMed: 21586578
DOI: 10.1074/JBC.M111.238931

実験手法

X-RAY DIFFRACTION (1.8 Å)