Homology among MurC, MurD, MurE and MurF proteins in Escherichia coli and that between E. coli MurG and a possible MurG protein in Bacillus subtilis.

Abstract

Determination of nucleotide sequence of a 2.8 kb DNA fragment involving the murG and murC genes has completed the sequencing of the total 12 kb mra region at 2 min on the Escherichia coli chromosome map, which functions in the growth and division of the cell. Product proteins of the genes in the mra region have alsq been identified, of which the MurC and MurG proteins are reported here. Considerable homologies were found in the deduced amino acid sequences of four ligases, products of the murC, murD, murE and murF genes in the mra region. These synthesize UDP-1V acetylmuramyl-pentapeptide from UDP-N acetylmuramic acid in peptidoglycan synthesis. The MurG protein, also involved in the cell growth of E. coli, showed considerable homology of the deduced amino acid sequence with that of a peptide coded for by an open reading frame in the spoVE ftsZ region of the B. subtilis chromosome.The mra (murein synthesis cluster a) region at 2 min on the Escherichia coli chromosome map carrying the genes for peptidoglycan synthesis was first found by Matsuzawa et al. (15) and the genes involved in this cluster have been investigated further in several laboratories (5,9,15,19,25,31). Genes coding for five enzymes, which synthesize UDP-N-acetylmuramyl-pentapeptide(L-alanyl-D-glutamyl-mesodiaminopimelyl-D-alanyl-D-alanine) from UDP-1V acetylmuramic acid by sequential addition of appropriate amino acids, have been located and aligned in this region. Independent lines of investigations (13,22,23,29) to identify genes responsible for

Crystal structure of UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase from Escherichia coli

“…Sequence homology has been reported previously for the four ligases of E.coli : MurC, MurD, MurE and MurF (Ikeda et al ., 1990b). Using the structural information obtained for MurD, the alignment of the four enzymes was repeated moving potential insertions into loop regions whenever possible.…”

Structural and Functional Characterization of Enantiomeric Glutamic Acid Derivatives as Potential Transition State Analogue Inhibitors of MurD Ligase

“…The ATP-binding pocket in particular seems to be well conserved throughout the family. [11][12][13] The catalytic mechanisms of Mur ligases have been studied at length and they most likely operate by an essentially similar mechanism. 1 After initial phosphorylation of the terminal carboxyl group of the UDP-substrate, the resulting acyl-phosphate is attacked by the amine moiety of the condensing amino acid residue.…”

Targeted molecular dynamics simulation studies of binding and conformational changes in E. coli MurD

“…Despite the surprising fact that sequence alignment of Mur ligase orthologs and paralogs showed relatively low overall homology alignment comparison of the residues comprising the active sites reached quite high homology scores. The ATP binding pocket in particular seems to be well conserved throughout the family 10, 11…”