4BUC

CRYSTAL STRUCTURE OF MURD LIGASE FROM THERMOTOGA MARITIMA IN APO FORM

4BUC の概要

• エントリーDOI: 10.2210/pdb4buc/pdb
• 関連するPDBエントリー: 4BUB
• 分子名称: UDP-N-ACETYLMURAMOYLALANINE--D-GLUTAMATE LIGASE, PHOSPHATE ION, PHOSPHITE ION, ... (7 entities in total)
• 機能のキーワード: ligase, peptidoglycan synthesis, adp-forming enzyme, cell wall, cell shape, cell cycle, nucleotide-binding, atp-binding, cell division
• 由来する生物種: THERMOTOGA MARITIMA
• 細胞内の位置: Cytoplasm (By similarity): Q9WY76
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 106574.71

構造登録者

Favini-Stabile, S.,Contreras-Martel, C.,Thielens, N.,Dessen, A. (登録日: 2013-06-20, 公開日: 2013-07-17, 最終更新日: 2024-10-09)

主引用文献

Favini-Stabile, S.,Contreras-Martel, C.,Thielens, N.,Dessen, A.
Mreb and Murg as Scaffolds for the Cytoplasmic Steps of Peptidoglycan Biosynthesis
Environ.Microbiol., 15:3218-, 2013

PubMed Abstract: Peptidoglycan is a major determinant of cell shape in bacteria, and its biosynthesis involves the concerted action of cytoplasmic, membrane-associated and periplasmic enzymes. Within the cytoplasm, Mur enzymes catalyse the first steps leading to peptidoglycan precursor biosynthesis, and have been suggested as being part of a multicomponent complex that could also involve the transglycosylase MurG and the cytoskeletal protein MreB. In order to initialize the characterization of a potential Mur interaction network, we purified MurD, MurE, MurF, MurG and MreB from Thermotoga maritima and characterized their interactions using membrane blotting and surface plasmon resonance. MurD, MurE and MurF all recognize MurG and MreB, but not each other, while the two latter proteins interact. In addition, we solved the crystal structures of MurD, MurE and MurF, which indicate that their C-termini display high conformational flexibilities. The differences in Mur conformations could be important parameters for the stability of an intracytoplasmic murein biosynthesis complex.

PubMed: 23826965
DOI: 10.1111/1462-2920.12171

実験手法

X-RAY DIFFRACTION (2.17 Å)