Crystal structures of active fully assembled substrate- and product-bound complexes of UDP-N-acetylmuramic acid:L-alanine ligase (MurC) from Haemophilus influenzae.

@article{Mol2003CrystalSO,
  title={Crystal structures of active fully assembled substrate- and product-bound complexes of UDP-N-acetylmuramic acid:L-alanine ligase (MurC) from Haemophilus influenzae.},
  author={C. De Mol and Alexei Brooun and Douglas R. Dougan and Mark T Hilgers and Leslie W. Tari and Robert A. Wijnands and Mark W. Knuth and Duncan E. McRee and Ronald V. Swanson},
  journal={Journal of bacteriology},
  year={2003},
  volume={185 14},
  pages={4152-62}
}
UDP-N-acetylmuramic acid:L-alanine ligase (MurC) catalyzes the addition of the first amino acid to the cytoplasmic precursor of the bacterial cell wall peptidoglycan. The crystal structures of Haemophilus influenzae MurC in complex with its substrate UDP-N-acetylmuramic acid (UNAM) and Mg(2+) and of a fully assembled MurC complex with its product UDP-N-acetylmuramoyl-L-alanine (UMA), the nonhydrolyzable ATP analogue AMPPNP, and Mn(2+) have been determined to 1.85- and 1.7-A resolution… CONTINUE READING

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