8B2H

Muramidase from Thermothielavioides terrestris, catalytic domain

8B2H の概要

• エントリーDOI: 10.2210/pdb8b2h/pdb
• 分子名称: SH3b domain-containing protein, 1,2-ETHANEDIOL, ZINC ION, ... (4 entities in total)
• 機能のキーワード: sh3-like, muramidase, peptidoglycan, cell wall binding domain, hydrolase
• 由来する生物種: Thermothielavioides terrestris
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 24054.72

構造登録者

Moroz, O.V.,Blagova, E.,Lebedev, A.A.,Skov, L.K.,Pache, R.A.,Schnorr, K.M.,Kiemer, L.,Nymand-Grarup, S.,Ming, L.,Ye, L.,Klausen, M.,Cohn, M.T.,Schmidt, E.G.W.,Davies, G.J.,Wilson, K.S. (登録日: 2022-09-13, 公開日: 2023-07-19, 最終更新日: 2024-11-06)

主引用文献

Moroz, O.V.,Blagova, E.,Lebedev, A.A.,Skov, L.K.,Pache, R.A.,Schnorr, K.M.,Kiemer, L.,Friis, E.P.,Nymand-Grarup, S.,Ming, L.,Ye, L.,Klausen, M.,Cohn, M.T.,Schmidt, E.G.W.,Davies, G.J.,Wilson, K.S.
Module walking using an SH3-like cell-wall-binding domain leads to a new GH184 family of muramidases.
Acta Crystallogr D Struct Biol, 79:706-720, 2023

PubMed Abstract: Muramidases (also known as lysozymes) hydrolyse the peptidoglycan component of the bacterial cell wall and are found in many glycoside hydrolase (GH) families. Similar to other glycoside hydrolases, muramidases sometimes have noncatalytic domains that facilitate their interaction with the substrate. Here, the identification, characterization and X-ray structure of a novel fungal GH24 muramidase from Trichophaea saccata is first described, in which an SH3-like cell-wall-binding domain (CWBD) was identified by structure comparison in addition to its catalytic domain. Further, a complex between a triglycine peptide and the CWBD from T. saccata is presented that shows a possible anchor point of the peptidoglycan on the CWBD. A `domain-walking' approach, searching for other sequences with a domain of unknown function appended to the CWBD, was then used to identify a group of fungal muramidases that also contain homologous SH3-like cell-wall-binding modules, the catalytic domains of which define a new GH family. The properties of some representative members of this family are described as well as X-ray structures of the independent catalytic and SH3-like domains of the Kionochaeta sp., Thermothielavioides terrestris and Penicillium virgatum enzymes. This work confirms the power of the module-walking approach, extends the library of known GH families and adds a new noncatalytic module to the muramidase arsenal.

PubMed: 37428847
DOI: 10.1107/S2059798323005004

実験手法

X-RAY DIFFRACTION (2.36 Å)