6TAB

Bd0314 DslA wild-type form 2

6TAB の概要

• エントリーDOI: 10.2210/pdb6tab/pdb
• 関連するPDBエントリー: 6TA9
• 分子名称: SLT domain-containing protein, SULFATE ION (3 entities in total)
• 機能のキーワード: lysozyme peptidoglycan, hydrolase
• 由来する生物種: Bdellovibrio bacteriovorus HD100
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 28089.54

構造登録者

Lovering, A.L.,Harding, C.J. (登録日: 2019-10-29, 公開日: 2020-07-15, 最終更新日: 2024-11-20)

主引用文献

Harding, C.J.,Huwiler, S.G.,Somers, H.,Lambert, C.,Ray, L.J.,Till, R.,Taylor, G.,Moynihan, P.J.,Sockett, R.E.,Lovering, A.L.
A lysozyme with altered substrate specificity facilitates prey cell exit by the periplasmic predator Bdellovibrio bacteriovorus.
Nat Commun, 11:4817-4817, 2020

PubMed Abstract: Lysozymes are among the best-characterized enzymes, acting upon the cell wall substrate peptidoglycan. Here, examining the invasive bacterial periplasmic predator Bdellovibrio bacteriovorus, we report a diversified lysozyme, DslA, which acts, unusually, upon (GlcNAc-) deacetylated peptidoglycan. B. bacteriovorus are known to deacetylate the peptidoglycan of the prey bacterium, generating an important chemical difference between prey and self walls and implying usage of a putative deacetyl-specific "exit enzyme". DslA performs this role, and ΔDslA strains exhibit a delay in leaving from prey. The structure of DslA reveals a modified lysozyme superfamily fold, with several adaptations. Biochemical assays confirm DslA specificity for deacetylated cell wall, and usage of two glutamate residues for catalysis. Exogenous DslA, added ex vivo, is able to prematurely liberate B. bacteriovorus from prey, part-way through the predatory lifecycle. We define a mechanism for specificity that invokes steric selection, and use the resultant motif to identify wider DslA homologues.

PubMed: 32968056
DOI: 10.1038/s41467-020-18139-8

実験手法

X-RAY DIFFRACTION (1.26 Å)