Description
Experimental Technique/Method:X-RAY DIFFRACTION
Resolution:1.8
Classification:SUGAR BINDING PROTEIN
Release Date:2016-01-27
Deposition Date:2015-11-12
Revision Date:2016-02-17#2016-04-13#2017-09-20
Molecular Weight:44843.57
Macromolecule Type:Protein
Residue Count:402
Atom Site Count:3103
DOI:10.2210/pdb5eq2/pdb
Abstract:
Streptococcus sanguinisis a leading cause of infective endocarditis, a life-threatening infection of the cardiovascular system. An important interaction in the pathogenesis of infective endocarditis is attachment of the organisms to host platelets.S. sanguinisexpresses a serine-rich repeat adhesin, SrpA, similar in sequence to platelet-binding adhesins associated with increased virulence in this disease. In this study, we determined the first crystal structure of the putative binding region of SrpA (SrpABR) both unliganded and in complex with a synthetic disaccharide ligand at 1.8 and 2.0 Å resolution, respectively. We identified a conserved Thr-Arg motif that orients the sialic acid moiety and is required for binding to platelet monolayers. Furthermore, we propose that sequence insertions in closely related family members contribute to the modulation of structural and functional properties, including the quaternary structure, the tertiary structure, and the ligand-binding site.
Resolution:1.8
Classification:SUGAR BINDING PROTEIN
Release Date:2016-01-27
Deposition Date:2015-11-12
Revision Date:2016-02-17#2016-04-13#2017-09-20
Molecular Weight:44843.57
Macromolecule Type:Protein
Residue Count:402
Atom Site Count:3103
DOI:10.2210/pdb5eq2/pdb
Abstract:
Streptococcus sanguinisis a leading cause of infective endocarditis, a life-threatening infection of the cardiovascular system. An important interaction in the pathogenesis of infective endocarditis is attachment of the organisms to host platelets.S. sanguinisexpresses a serine-rich repeat adhesin, SrpA, similar in sequence to platelet-binding adhesins associated with increased virulence in this disease. In this study, we determined the first crystal structure of the putative binding region of SrpA (SrpABR) both unliganded and in complex with a synthetic disaccharide ligand at 1.8 and 2.0 Å resolution, respectively. We identified a conserved Thr-Arg motif that orients the sialic acid moiety and is required for binding to platelet monolayers. Furthermore, we propose that sequence insertions in closely related family members contribute to the modulation of structural and functional properties, including the quaternary structure, the tertiary structure, and the ligand-binding site.
| Date made available | 2016 |
|---|---|
| Publisher | RCSB-PDB |