3K3P

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

Summary for 3K3P

• Entry DOI: 10.2210/pdb3k3p/pdb
• Descriptor: D-alanine--D-alanine ligase (2 entities in total)
• Functional Keywords: d-alanyl-alanine synthetase, atp-binding, cell shape, cell wall biogenesis/degradation, ligase, magnesium, manganese, metal-binding, nucleotide-binding, peptidoglycan synthesis
• Biological source: Streptococcus mutans
• Total number of polymer chains: 2
• Total formula weight: 84848.55

Authors

Lu, Y. (deposition date: 2009-10-03, release date: 2010-09-15, Last modification date: 2023-11-01)

Primary citation

Lu, Y.,Xu, H.,Zhao, X.
Crystal structure of the Apo form of D-Alanine:D-Alanine ligase (DDl) from Streptococcus mutans.
Protein Pept.Lett., 17:1053-1057, 2010

PubMed 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 A 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 omega-loop region.

PubMed: 20522004
DOI: 10.2174/092986610791498858

Experimental method

X-RAY DIFFRACTION (2.23 Å)