1j6u

Protein Summary

The TM0231 gene of Thermotoga maritima encodes an UDP-N-acetylmuramate-alanine ligase (MurC; EC 6.3.2.8; COG0773) that is involved in the biosynthesis of the peptidoglycan murein, a major component of the bacterial cell wall (PubMed:15146505). Genes for the peptidoglycan synthesis pathway are also essential for chloroplast division in moss (PubMed:16618924).

Detailed knowledge of the chemistry and structural features of the murein network is important as the mode of action of the ?-lactam antibiotics, the most important group of antibacterial drugs, and the mechanisms that the bacteria have developed to survive in the presence of these antibiotics, are related to the biosynthesis, three-dimensional structure and morphogenesis of the peptidoglycans.

There are three domains in the structure of TM0231:
(a) MurCD N-terminal domain (SCOP sunid:51983) with 3 layers: a/b/a; parallel beta-sheet of 5 strands, order 32145; incomplete Rossmann-like fold; binds UDP group;
(b) peptide-binding domain with fold of MurD-like peptide ligases (SCOP sunid 53243) with 3 layers: a/b/a; mixed beta-sheet of 6 strands, order 126345; strand 1 is antiparallel to the rest
(c) domain with Ribokinase-like fold (SCOP sunid:53612) with core: 3 layers: a/b/a; mixed beta-sheet of 8 strands, order 21345678, strand 7 is antiparallel to the rest; potential superfamily: members of this fold have similar functions but different ATP-binding sites.

Using FATCAT server structures similar to TM0231 were found  in PDB (i.e.: 1gqqA, 1e0dA, 1e8cA, 1gg4A, 2am1A, 1w78A, 1fgs_, and 1o5zA). There is also significant sequence similarity (analyzed with FFAS03 server) between those structures and TM0231.