3ZRZ
Crystal structure of the second and third fibronectin F1 modules in complex with a fragment of Streptococcus pyogenes SfbI-5
Summary for 3ZRZ
| Entry DOI | 10.2210/pdb3zrz/pdb |
| Related | 1E88 1E8B 1FBR 1FNA 1FNF 1FNH 1J8K 1O9A 1OWW 1Q38 1QGB 1QO6 1TTF 1TTG 2CG6 2CG7 2CK2 2CKU 2FN2 2FNB |
| Descriptor | FIBRONECTIN, FIBRONECTIN-BINDING PROTEIN, SULFATE ION, ... (5 entities in total) |
| Functional Keywords | cell adhesion, prtf, beta zipper |
| Biological source | HOMO SAPIENS (HUMAN) More |
| Total number of polymer chains | 4 |
| Total formula weight | 24425.32 |
| Authors | Norris, N.C.,Bingham, R.J.,Potts, J.R. (deposition date: 2011-06-21, release date: 2011-09-28, Last modification date: 2024-11-06) |
| Primary citation | Norris, N.C.,Bingham, R.J.,Harris, G.,Speakman, A.,Jones, R.P.O.,Leech, A.,Turkenburg, J.P.,Potts, J.R. Structural and Functional Analysis of the Tandem Beta-Zipper Interaction of a Streptococcal Protein with Human Fibronectin. J.Biol.Chem., 286:38311-, 2011 Cited by PubMed Abstract: Bacterial fibronectin-binding proteins (FnBPs) contain a large intrinsically disordered region (IDR) that mediates adhesion of bacteria to host tissues, and invasion of host cells, through binding to fibronectin (Fn). These FnBP IDRs consist of Fn-binding repeats (FnBRs) that form a highly extended tandem β-zipper interaction on binding to the N-terminal domain of Fn. Several FnBR residues are highly conserved across bacterial species, and here we investigate their contribution to the interaction. Mutation of these residues to alanine in SfbI-5 (a disordered FnBR from the human pathogen Streptococcus pyogenes) reduced binding, but for each residue the change in free energy of binding was <2 kcal/mol. The structure of an SfbI-5 peptide in complex with the second and third F1 modules from Fn confirms that the conserved FnBR residues play equivalent functional roles across bacterial species. Thus, in SfbI-5, the binding energy for the tandem β-zipper interaction with Fn is distributed across the interface rather than concentrated in a small number of "hot spot" residues that are frequently observed in the interactions of folded proteins. We propose that this might be a common feature of the interactions of IDRs and is likely to pose a challenge for the development of small molecule inhibitors of FnBP-mediated adhesion to and invasion of host cells. PubMed: 21840989DOI: 10.1074/JBC.M111.276592 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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