1JMM

Crystal structure of the V-region of Streptococcus mutans antigen I/II

Summary for 1JMM

• Entry DOI: 10.2210/pdb1jmm/pdb
• Descriptor: protein I/II V-region, SODIUM ION (3 entities in total)
• Functional Keywords: antigen i/ii, v-region, immune system, membrane protein
• Biological source: Streptococcus mutans
• Cellular location: Secreted, cell wall; Peptidoglycan-anchor (Potential): P11657
• Total number of polymer chains: 1
• Total formula weight: 41638.11

Authors

Troffer-Charlier, N.,Ogier, J.,Moras, D.,Cavarelli, J. (deposition date: 2001-07-19, release date: 2002-07-17, Last modification date: 2024-11-06)

Primary citation

Troffer-Charlier, N.,Ogier, J.,Moras, D.,Cavarelli, J.
Crystal Structure of the V-region of Streptococcus mutans Antigen I/II at 2.4 a Resolution Suggests a Sugar Preformed Binding Site
J.Mol.Biol., 318:179-188, 2002

PubMed Abstract: Antigens I/II are large multifunctional adhesins from oral viridans streptococci that exert immunomodulatory effects on human cells and play important roles in inflammatory disorders. Among them, Streptococcus mutans plays a major role in the initiation of dental caries. The structure of the V-region (SrV+, residues 464-840) of the antigen I/II of S. mutans has been determined using the multiwavelength anomalous diffraction phasing technique with seleno-methionine-substituted recombinant protein and subsequently refined at 2.4 A resolution. The crystal structure of SrV+ revealed a lectin-like fold that displays a putative preformed carbohydrate-binding site stabilized by a metal ion. Inhibition of this binding site may confer to humans a protection against dental caries and dissemination of the bacteria to extra-oral sites involved in life-threatening inflammatory diseases. This crystal structure constitutes a first step in understanding the structure-function relationship of antigens I/II and may help in delineating new preventive or therapeutic strategies against colonization of the host by oral streptococci.

PubMed: 12054777
DOI: 10.1016/S0022-2836(02)00025-6

Experimental method

X-RAY DIFFRACTION (2.4 Å)