2F00

Escherichia coli MurC

2F00 の概要

• エントリーDOI: 10.2210/pdb2f00/pdb
• 分子名称: UDP-N-acetylmuramate--L-alanine ligase, MAGNESIUM ION (3 entities in total)
• 機能のキーワード: amide bond ligase, atpase, bacterial cell wall, ligase
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cytoplasm (Probable): P17952
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 108832.98

構造登録者

Deva, T.,Baker, E.N.,Squire, C.J.,Smith, C.A. (登録日: 2005-11-10, 公開日: 2006-10-24, 最終更新日: 2024-11-20)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.5 Å)