1E8C

Structure of MurE the UDP-N-acetylmuramyl tripeptide synthetase from E. coli

Summary for 1E8C

• Entry DOI: 10.2210/pdb1e8c/pdb
• Descriptor: UDP-N-ACETYLMURAMOYLALANYL-D-GLUTAMATE--2,6-DIAMINOPIMELATE LIGASE, CHLORIDE ION, URIDINE-5'-DIPHOSPHATE-N-ACETYLMURAMOYL-L-ALANINE-D-GLUTAMATE, ... (5 entities in total)
• Functional Keywords: ligase, peptidoglycan biosynthesis
• Biological source: ESCHERICHIA COLI
• Total number of polymer chains: 2
• Total formula weight: 110978.13

Authors

Gordon, E.J.,Chantala, L.,Dideberg, O. (deposition date: 2000-09-19, release date: 2001-09-13, Last modification date: 2023-11-15)

Primary citation

Gordon, E.J.,Flouret, B.,Chantalat, L.,Van Heijenoort, J.,Mengin-Lecreulx, D.,Dideberg, O.
Crystal Structure of Udp-N-Acetylmuramoyl-L-Alanyl-D-Glutamate: Meso-Diaminopimelate Ligase from Escherichia Coli
J.Biol.Chem., 276:10999-, 2001

PubMed Abstract: UDP-N-acetylmuramoyl-l-alanyl-d-glutamate:meso-diaminopimelate ligase is a cytoplasmic enzyme that catalyzes the addition of meso-diaminopimelic acid to nucleotide precursor UDP-N-acetylmuramoyl-l-alanyl-d-glutamate in the biosynthesis of bacterial cell-wall peptidoglycan. The crystal structure of the Escherichia coli enzyme in the presence of the final product of the enzymatic reaction, UDP-MurNAc-l-Ala-gamma-d-Glu-meso-A(2)pm, has been solved to 2.0 A resolution. Phase information was obtained by multiwavelength anomalous dispersion using the K shell edge of selenium. The protein consists of three domains, two of which have a topology reminiscent of the equivalent domain found in the already established three-dimensional structure of the UDP-N-acetylmuramoyl-l-alanine: D-glutamate-ligase (MurD) ligase, which catalyzes the immediate previous step of incorporation of d-glutamic acid in the biosynthesis of the peptidoglycan precursor. The refined model reveals the binding site for UDP-MurNAc-l-Ala-gamma-d-Glu-meso-A(2)pm, and comparison with the six known MurD structures allowed the identification of residues involved in the enzymatic mechanism. Interestingly, during refinement, an excess of electron density was observed, leading to the conclusion that, as in MurD, a carbamylated lysine residue is present in the active site. In addition, the structural determinant responsible for the selection of the amino acid to be added to the nucleotide precursor was identified.

PubMed: 11124264
DOI: 10.1074/JBC.M009835200

Experimental method

X-RAY DIFFRACTION (2 Å)