4X36

Crystal structure of the autolysin LytA from Streptococcus pneumoniae TIGR4

Summary for 4X36

• Entry DOI: 10.2210/pdb4x36/pdb
• Descriptor: Autolysin, GLYCEROL, ZINC ION, ... (5 entities in total)
• Functional Keywords: autolysin, amidase, hydrolase
• Biological source: Streptococcus pneumoniae TIGR4
• Cellular location: Secreted : P06653
• Total number of polymer chains: 1
• Total formula weight: 38053.35

Authors

Cheng, W.,Li, Q.,Zhou, C.Z.,Chen, Y.X. (deposition date: 2014-11-28, release date: 2015-05-27, Last modification date: 2024-10-30)

Primary citation

Li, Q.,Cheng, W.,Morlot, C.,Bai, X.H.,Jiang, Y.L.,Wang, W.,Roper, D.I.,Vernet, T.,Dong, Y.H.,Chen, Y.,Zhou, C.Z.
Full-length structure of the major autolysin LytA.
Acta Crystallogr.,Sect.D, 71:1373-1381, 2015

PubMed Abstract: LytA is responsible for the autolysis of many Streptococcus species, including pathogens such as S. pneumoniae, S. pseudopneumoniae and S. mitis. However, how this major autolysin achieves full activity remains unknown. Here, the full-length structure of the S. pneumoniae LytA dimer is reported at 2.1 Å resolution. Each subunit has an N-terminal amidase domain and a C-terminal choline-binding domain consisting of six choline-binding repeats, which form five canonical and one single-layered choline-binding sites. Site-directed mutageneses combined with enzymatic activity assays indicate that dimerization and binding to choline are two independent requirements for the autolytic activity of LytA in vivo. Altogether, it is suggested that dimerization and full occupancy of all choline-binding sites through binding to choline-containing TA chains enable LytA to adopt a fully active conformation which allows the amidase domain to cleave two lactyl-amide bonds located about 103 Å apart on the peptidoglycan.

PubMed: 26057677
DOI: 10.1107/S1399004715007403

Experimental method

X-RAY DIFFRACTION (2.101 Å)