3ZRZ

Crystal structure of the second and third fibronectin F1 modules in complex with a fragment of Streptococcus pyogenes SfbI-5

3ZRZ の概要

• エントリーDOI: 10.2210/pdb3zrz/pdb
• 関連するPDBエントリー: 1E88 1E8B 1FBR 1FNA 1FNF 1FNH 1J8K 1O9A 1OWW 1Q38 1QGB 1QO6 1TTF 1TTG 2CG6 2CG7 2CK2 2CKU 2FN2 2FNB
• 分子名称: FIBRONECTIN, FIBRONECTIN-BINDING PROTEIN, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: cell adhesion, prtf, beta zipper
• 由来する生物種: HOMO SAPIENS (HUMAN); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 24425.32

構造登録者

Norris, N.C.,Bingham, R.J.,Potts, J.R. (登録日: 2011-06-21, 公開日: 2011-09-28, 最終更新日: 2024-11-06)

主引用文献

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

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: 21840989
DOI: 10.1074/JBC.M111.276592

実験手法

X-RAY DIFFRACTION (1.7 Å)