2F00

Escherichia coli MurC

Summary for 2F00

• Entry DOI: 10.2210/pdb2f00/pdb
• Descriptor: UDP-N-acetylmuramate--L-alanine ligase, MAGNESIUM ION (3 entities in total)
• Functional Keywords: amide bond ligase, atpase, bacterial cell wall, ligase
• Biological source: Escherichia coli
• Cellular location: Cytoplasm (Probable): P17952
• Total number of polymer chains: 2
• Total formula weight: 108832.98

Authors

Deva, T.,Baker, E.N.,Squire, C.J.,Smith, C.A. (deposition date: 2005-11-10, release date: 2006-10-24, Last modification date: 2024-11-20)

Primary citation

Deva, T.,Baker, E.N.,Squire, C.J.,Smith, C.A.
Structure of Escherichia coliUDP-N-acetylmuramoyl:L-alanine ligase (MurC).
Acta Crystallogr.,Sect.D, 62:1466-1474, 2006

PubMed Abstract: The bacterial cell wall provides essential protection from the external environment and confers strength and rigidity to counteract internal osmotic pressure. Without this layer the cell would be easily ruptured and it is for this reason that biosynthetic pathways leading to the formation of peptidoglycan have for many years been a prime target for effective antibiotics. Central to this pathway are four similar ligase enzymes which add peptide groups to glycan moieties. As part of a program to better understand the structure-function relationships in these four enzymes, the crystal structure of Escherichia coli UDP-N-acetylmuramoyl:L-alanine ligase (MurC) has been determined to 2.6 A resolution. The structure was solved by multiwavelength anomalous diffraction methods from a single selenomethionine-substituted crystal and refined to a crystallographic R factor of 0.212 (R(free) = 0.259). The enzyme has a modular multi-domain structure very similar to those of other members of the mur family of ATP-dependent amide-bond ligases. Detailed comparison of these four enzymes shows that considerable conformational changes are possible. These changes, together with the recruitment of two different N-terminal domains, allow this family of enzymes to bind a substrate which is identical at one end and at the other has the growing peptide tail which will ultimately become part of the rigid bacterial cell wall. Comparison of the E. coli and Haemophilus influenzae structures and analysis of the sequences of known MurC enzymes indicate the presence of a ;dimerization' motif in almost 50% of the MurC enzymes and points to a highly conserved loop in domain 3 that may play a key role in amino-acid ligand specificity.

PubMed: 17139082
DOI: 10.1107/S0907444906038376

Experimental method

X-RAY DIFFRACTION (2.5 Å)