The solution and crystal structures of a module pair from the Staphylococcus aureus-binding site of human fibronectin - A tale with a twist


Rudino-Pinera, E., Ravelli, R.B.G., Sheldrick, G.M., Nanao, M.H., Korostelev, V.V., Werner, J.M., Schwarz-Linek, U., Potts, J.R. and Garman, E.F. (2007) The solution and crystal structures of a module pair from the Staphylococcus aureus-binding site of human fibronectin - A tale with a twist. Journal of Molecular Biology, 368, (3), 833-844. (doi:10.1016/j.jmb.2007.02.061).

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Description/Abstract

An important goal of structural studies of modular proteins is to determine the inter-module orientation, which often influences biological function. The N-terminal domain of human fibronectin (Fn) is composed of a string of five type 1 modules (F1). Despite their small size, to date F1 modules have proved intractable to X-ray structure solution, although there are several NMR structures available. Here, we present the first structures (two X-ray models and an NMR-derived model) of the 2F13F1 module pair, which forms part of the binding site for Fn-binding proteins from pathogenic bacteria. The crystallographic structure determination was aided by the novel technique of UV radiation damage-induced phasing. The individual module structures are very similar in all three models. In the NMR structure and one of the X-ray structures, a similar but smaller interdomain interface than that observed previously for 4F15F1 is seen. The other X-ray structure has a different interdomain orientation. This work underlines the benefits of combining X-ray and NMR data in the studies of multi-domain proteins.

Item Type: Article
ISSNs: 0022-2836 (print)
Related URLs:
Keywords: fibronectin, crystallography, NMR, multidomains, domain orientation
Subjects: Q Science > Q Science (General)
R Medicine > R Medicine (General)
Divisions: University Structure - Pre August 2011 > School of Biological Sciences
ePrint ID: 56113
Date Deposited: 07 Aug 2008
Last Modified: 27 Mar 2014 18:38
URI: http://eprints.soton.ac.uk/id/eprint/56113

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