5EQ3
Crystal structure of the SrpA adhesin from Streptococcus sanguinis with a sialyl galactose disaccharide bound
Summary for 5EQ3
Entry DOI | 10.2210/pdb5eq3/pdb |
Related | 5EQ2 5EQ3 |
Descriptor | Platelet-binding glycoprotein, N-glycolyl-alpha-neuraminic acid-(2-3)-methyl beta-D-galactopyranoside, CALCIUM ION, ... (6 entities in total) |
Functional Keywords | bacterial adhesin, lectin, immunoglobulin fold, serine-rich repeat, sugar binding protein |
Biological source | Streptococcus sanguinis |
Total number of polymer chains | 2 |
Total formula weight | 45072.77 |
Authors | Loukachevitch, L.V.,McCulloch, K.M.,Vann, K.R.,Wawrzak, Z.,Anderson, S.,Iverson, T.M. (deposition date: 2015-11-12, release date: 2016-01-27, Last modification date: 2024-03-06) |
Primary citation | Bensing, B.A.,Loukachevitch, L.V.,McCulloch, K.M.,Yu, H.,Vann, K.R.,Wawrzak, Z.,Anderson, S.,Chen, X.,Sullam, P.M.,Iverson, T.M. Structural Basis for Sialoglycan Binding by the Streptococcus sanguinis SrpA Adhesin. J.Biol.Chem., 291:7230-7240, 2016 Cited by PubMed 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. PubMed: 26833566DOI: 10.1074/jbc.M115.701425 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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