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3ZL8

CRYSTAL STRUCTURE OF MURF LIGASE FROM THERMOTOGA MARITIMA IN COMPLEX WITH ADP

Summary for 3ZL8
Entry DOI10.2210/pdb3zl8/pdb
DescriptorUDP-N-ACETYLMURAMOYL-TRIPEPTIDE--D-ALANYL-D-ALANINE LIGASE, GLYCEROL, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
Functional Keywordsligase, peptidoglycan synthesis, adp-forming enzyme, cell wall, cell shape, cell cycle, nucleotide-binding, atp-binding, cell division
Biological sourceTHERMOTOGA MARITIMA
Cellular locationCytoplasm (By similarity): Q9WY78
Total number of polymer chains1
Total formula weight49770.78
Authors
Favini-Stabile, S.,Contreras-Martel, C.,Thielens, N.,Dessen, A. (deposition date: 2013-01-29, release date: 2013-09-11, Last modification date: 2024-05-08)
Primary citationFavini-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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.65 Å)
Structure validation

230083

건을2025-01-15부터공개중

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