2RL0

Crystal structure of the fourth and fifth fibronectin F1 modules in complex with a fragment of staphylococcus aureus fnbpa-5

Summary for 2RL0

• Entry DOI: 10.2210/pdb2rl0/pdb
• Related: 2RKY 2RKZ 3CAL
• Descriptor: Fibronectin, Fibronectin-binding protein (3 entities in total)
• Functional Keywords: fibronectin, 4f15f1, beta zipper, staphylococcus aureus, acute phase, alternative splicing, cell adhesion, extracellular matrix, glycoprotein, heparin-binding, phosphorylation, pyrrolidone carboxylic acid, secreted, sulfation, cell wall, peptidoglycan-anchor, virulence
• Biological source: Homo sapiens (human); More
• Cellular location: Secreted, extracellular space, extracellular matrix: P02751; Secreted, cell wall; Peptidoglycan-anchor (Potential): P14738
• Total number of polymer chains: 12
• Total formula weight: 72908.25

Authors

Bingham, R.J. (deposition date: 2007-10-18, release date: 2008-08-05, Last modification date: 2024-10-30)

Primary citation

Bingham, R.J.,Meenan, N.A.,Schwarz-Linek, U.,Turkenburg, J.P.,Garman, E.F.,Potts, J.R.
Crystal structures of fibronectin-binding sites from Staphylococcus aureus FnBPA in complex with fibronectin domains
Proc.Natl.Acad.Sci.Usa, 105:12254-12258, 2008

PubMed Abstract: Staphylococcus aureus can adhere to and invade endothelial cells by binding to the human protein fibronectin (Fn). FnBPA and FnBPB, cell wall-attached proteins from S. aureus, have multiple, intrinsically disordered, high-affinity binding repeats (FnBRs) for Fn. Here, 30 years after the first report of S. aureus/Fn interactions, we present four crystal structures that together comprise the structures of two complete FnBRs, each in complex with four of the N-terminal modules of Fn. Each approximately 40-residue FnBR forms antiparallel strands along the triple-stranded beta-sheets of four sequential F1 modules ((2-5)F1) with each FnBR/(2-5)F1 interface burying a total surface area of approximately 4,300 A(2). The structures reveal the roles of residues conserved between S. aureus and Streptococcus pyogenes FnBRs and show that there are few linker residues between FnBRs. The ability to form large intermolecular interfaces with relatively few residues has been proposed to be a feature of disordered proteins, and S. aureus/Fn interactions provide an unusual illustration of this efficiency.

PubMed: 18713862
DOI: 10.1073/pnas.0803556105

Experimental method

X-RAY DIFFRACTION (2 Å)