2WWD

3D-structure of the modular autolysin LytC from Streptococcus pneumoniae in complex with pneummococcal peptidoglycan fragment

Summary for 2WWD

• Entry DOI: 10.2210/pdb2wwd/pdb
• Related: 2WW5 2WWC
• Descriptor: 1,4-BETA-N-ACETYLMURAMIDASE, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-N-acetyl-alpha-muramic acid, GLYCEROL, ... (7 entities in total)
• Functional Keywords: hydrolase, glycosidase, choline-binding proteins
• Biological source: STREPTOCOCCUS PNEUMONIAE
• Total number of polymer chains: 1
• Total formula weight: 57376.19

Authors

Perez-Dorado, I.,Sanles, R.,Hermoso, J.A.,Gonzalez, A.,Garcia, A.,Garcia, P.,Garcia, J.L. (deposition date: 2009-10-22, release date: 2010-04-21, Last modification date: 2023-12-20)

Primary citation

Perez-Dorado, I.,Gonzalez, A.,Morales, M.,Sanles, R.,Striker, W.,Vollmer, W.,Mobashery, S.,Garcia, J.L.,Martinez-Ripoll, M.,Garcia, P.,Hermoso, J.A.
Insights Into Pneumococcal Fratricide from the Crystal Structures of the Modular Killing Factor Lytc.
Nat.Struct.Mol.Biol., 17:576-, 2010

PubMed Abstract: The first structure of a pneumococcal autolysin, that of the LytC lysozyme, has been solved in ternary complex with choline and a pneumococcal peptidoglycan (PG) fragment. The active site of the hydrolase module is not fully exposed but is oriented toward the choline-binding module, which accounts for its unique in vivo features in PG hydrolysis, its activation and its regulatory mechanisms. Because of the unusual hook-shaped conformation of the multimodular protein, it is only able to hydrolyze non-cross-linked PG chains, an assertion validated by additional experiments. These results explain the activation of LytC by choline-binding protein D (CbpD) in fratricide, a competence-programmed mechanism of predation of noncompetent sister cells. The results provide the first structural insights to our knowledge into the critical and central function that LytC plays in pneumococcal virulence and explain a long-standing puzzle of how murein hydrolases can be controlled to avoid self-lysis during bacterial growth and division.

PubMed: 20400948
DOI: 10.1038/NSMB.1817

Experimental method

X-RAY DIFFRACTION (2.25 Å)