4IGB
Crystal structure of the N-terminal domain of the Streptococcus gordonii adhesin Sgo0707
Summary for 4IGB
| Entry DOI | 10.2210/pdb4igb/pdb |
| Descriptor | LPXTG cell wall surface protein, SULFATE ION, GLYCEROL, ... (9 entities in total) |
| Functional Keywords | beta-sandwich folds, adhesin, collagen-binding, oral keratinocytes, cell wall anchored protein, cell adhesion |
| Biological source | Streptococcus gordonii More |
| Total number of polymer chains | 4 |
| Total formula weight | 193951.46 |
| Authors | Nylander, A.,Svensater, G.,Senadheera, D.B.,Cvitkovitch, D.G.,Davies, J.R.,Persson, K. (deposition date: 2012-12-17, release date: 2013-06-05, Last modification date: 2024-03-20) |
| Primary citation | Nylander, A.,Svensater, G.,Senadheera, D.B.,Cvitkovitch, D.G.,Davies, J.R.,Persson, K. Structural and Functional Analysis of the N-terminal Domain of the Streptococcus gordonii Adhesin Sgo0707 Plos One, 8:e63768-e63768, 2013 Cited by PubMed Abstract: The commensal Streptococcus gordonii expresses numerous surface adhesins with which it interacts with other microorganisms, host cells and salivary proteins to initiate dental plaque formation. However, this Gram-positive bacterium can also spread to non-oral sites such as the heart valves and cause infective endocarditis. One of its surface adhesins, Sgo0707, is a large protein composed of a non-repetitive N-terminal region followed by several C-terminal repeat domains and a cell wall sorting motif. Here we present the crystal structure of the Sgo0707 N-terminal domains, refined to 2.1 Å resolution. The model consists of two domains, N1 and N2. The largest domain, N1, comprises a putative binding cleft with a single cysteine located in its centre and exhibits an unexpected structural similarity to the variable domains of the streptococcal Antigen I/II adhesins. The N2-domain has an IgG-like fold commonly found among Gram-positive surface adhesins. Binding studies performed on S. gordonii wild-type and a Sgo0707 deficient mutant show that the Sgo0707 adhesin is involved in binding to type-1 collagen and to oral keratinocytes. PubMed: 23691093DOI: 10.1371/journal.pone.0063768 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.09 Å) |
Structure validation
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