3ZL8
CRYSTAL STRUCTURE OF MURF LIGASE FROM THERMOTOGA MARITIMA IN COMPLEX WITH ADP
Summary for 3ZL8
Entry DOI | 10.2210/pdb3zl8/pdb |
Descriptor | UDP-N-ACETYLMURAMOYL-TRIPEPTIDE--D-ALANYL-D-ALANINE LIGASE, GLYCEROL, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total) |
Functional Keywords | ligase, peptidoglycan synthesis, adp-forming enzyme, cell wall, cell shape, cell cycle, nucleotide-binding, atp-binding, cell division |
Biological source | THERMOTOGA MARITIMA |
Cellular location | Cytoplasm (By similarity): Q9WY78 |
Total number of polymer chains | 1 |
Total formula weight | 49770.78 |
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 citation | 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 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: 23826965DOI: 10.1111/1462-2920.12171 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.65 Å) |
Structure validation
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