Crystal Structure of the Apo Form of D-Alanine:D-Alanine Ligase (DDl) from Streptococcus mutans

Title: Crystal Structure of the Apo Form of D-Alanine:D-Alanine Ligase (DDl) from Streptococcus mutans

Volume: 17 Issue: 8

Author(s): Yongzhi Lu, Hongyan Xu and Xiaojun Zhao

Affiliation:

Keywords: X-ray crystal structure, amino acids and peptides, DDl, Streptococcus mutans

Abstract: D-Alanine:D-Alanine ligase (DDl) catalyzes the formation of D-Alanine:D-Alanine dipeptide and is an essential enzyme in bacterial cell wall biosynthesis. This enzyme does not have a human ortholog, making it an attractive target for developing new antibiotic drugs. We determined the crystal structure at 2.23 Å resolution of DDl from Streptococcus mutans (SmDDl), the principal aetiological agent of human dental caries. This structure reveals that SmDDl is a dimer and has a disordered ω-loop region.

Cite this article as:

Lu Yongzhi, Xu Hongyan and Zhao Xiaojun, Crystal Structure of the Apo Form of D-Alanine:D-Alanine Ligase (DDl) from Streptococcus mutans, Protein & Peptide Letters 2010; 17 (8) . https://dx.doi.org/10.2174/092986610791498858