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

The solution and crystal structures of a module pair from the Staphylococcus aureus-binding site of human fibronectin - A tale with a twist
The solution and crystal structures of a module pair from the Staphylococcus aureus-binding site of human fibronectin - A tale with a twist
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.
fibronectin, crystallography, NMR, multidomains, domain orientation
0022-2836
833-844
Rudino-Pinera, E.
45f80d6c-c8ab-480b-a289-5b2f0ae42514
Ravelli, R.B.G.
6b975375-75e4-4928-a76a-47e228f45c33
Sheldrick, G.M.
e450a62b-a120-44c0-a6a6-aae93db3dbcf
Nanao, M.H.
a6400d7b-8e91-462c-be15-b1b3960c01f0
Korostelev, V.V.
67ee072e-20bc-40aa-a4b5-a71a99d794bb
Werner, J.M.
1b02513a-8310-4f4f-adac-dc2a466bd115
Schwarz-Linek, U.
88e96469-0179-4c9c-8f91-9a6e0e06f63a
Potts, J.R.
eaf16b7a-d162-4152-add0-ee112889c17f
Garman, E.F.
580e97e2-e145-428a-86ab-3e3b779f7ade
Rudino-Pinera, E.
45f80d6c-c8ab-480b-a289-5b2f0ae42514
Ravelli, R.B.G.
6b975375-75e4-4928-a76a-47e228f45c33
Sheldrick, G.M.
e450a62b-a120-44c0-a6a6-aae93db3dbcf
Nanao, M.H.
a6400d7b-8e91-462c-be15-b1b3960c01f0
Korostelev, V.V.
67ee072e-20bc-40aa-a4b5-a71a99d794bb
Werner, J.M.
1b02513a-8310-4f4f-adac-dc2a466bd115
Schwarz-Linek, U.
88e96469-0179-4c9c-8f91-9a6e0e06f63a
Potts, J.R.
eaf16b7a-d162-4152-add0-ee112889c17f
Garman, E.F.
580e97e2-e145-428a-86ab-3e3b779f7ade

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).

Record type: Article

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.

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More information

Published date: 4 May 2007
Keywords: fibronectin, crystallography, NMR, multidomains, domain orientation

Identifiers

Local EPrints ID: 56113
URI: http://eprints.soton.ac.uk/id/eprint/56113
ISSN: 0022-2836
PURE UUID: 32b651eb-ee91-4cbe-b491-96d4f6c468cb
ORCID for J.M. Werner: ORCID iD orcid.org/0000-0002-4712-1833

Catalogue record

Date deposited: 07 Aug 2008
Last modified: 16 Mar 2024 03:36

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Contributors

Author: E. Rudino-Pinera
Author: R.B.G. Ravelli
Author: G.M. Sheldrick
Author: M.H. Nanao
Author: V.V. Korostelev
Author: J.M. Werner ORCID iD
Author: U. Schwarz-Linek
Author: J.R. Potts
Author: E.F. Garman

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