5CEC

Bd3459 Predatory Endopeptidase from Bdellovibrio bacteriovorus in complex with immunity protein Bd3460

5CEC の概要

• エントリーDOI: 10.2210/pdb5cec/pdb
• 分子名称: Bd3459, Bd3460, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: transpeptidase and ankyrin repeat, protein binding
• 由来する生物種: Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIB 9529 / HD100); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 74551.25

構造登録者

Lovering, A.L.,Cadby, I.T.,Lambert, C.,Sockett, R.E. (登録日: 2015-07-06, 公開日: 2015-12-09, 最終更新日: 2024-11-13)

主引用文献

Lambert, C.,Cadby, I.T.,Till, R.,Bui, N.K.,Lerner, T.R.,Hughes, W.S.,Lee, D.J.,Alderwick, L.J.,Vollmer, W.,Sockett, E.R.,Lovering, A.L.
Ankyrin-mediated self-protection during cell invasion by the bacterial predator Bdellovibrio bacteriovorus.
Nat Commun, 6:8884-8884, 2015

PubMed Abstract: Predatory Bdellovibrio bacteriovorus are natural antimicrobial organisms, killing other bacteria by whole-cell invasion. Self-protection against prey-metabolizing enzymes is important for the evolution of predation. Initial prey entry involves the predator's peptidoglycan DD-endopeptidases, which decrosslink cell walls and prevent wasteful entry by a second predator. Here we identify and characterize a self-protection protein from B. bacteriovorus, Bd3460, which displays an ankyrin-based fold common to intracellular pathogens of eukaryotes. Co-crystal structures reveal Bd3460 complexation of dual targets, binding a conserved epitope of each of the Bd3459 and Bd0816 endopeptidases. Complexation inhibits endopeptidase activity and cell wall decrosslinking in vitro. Self-protection is vital - ΔBd3460 Bdellovibrio deleteriously decrosslink self-peptidoglycan upon invasion, adopt a round morphology, and lose predatory capacity and cellular integrity. Our analysis provides the first mechanistic examination of self-protection in Bdellovibrio, documents protection-multiplicity for products of two different genomic loci, and reveals an important evolutionary adaptation to an invasive predatory bacterial lifestyle.

PubMed: 26626559
DOI: 10.1038/ncomms9884

実験手法

X-RAY DIFFRACTION (1.36 Å)