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...
| Main Authors: | , , , , , , , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
2007
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| _version_ | 1797056120687165440 |
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| author | Rudiño-Piñera, E Ravelli, R Sheldrick, G Nanao, M Korostelev, V Werner, J Schwarz-Linek, U Potts, JR Garman, E |
| author_facet | Rudiño-Piñera, E Ravelli, R Sheldrick, G Nanao, M Korostelev, V Werner, J Schwarz-Linek, U Potts, JR Garman, E |
| author_sort | Rudiño-Piñera, E |
| collection | OXFORD |
| description | 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 (2)F1(3)F1 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 (4)F1(5)F1 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. |
| first_indexed | 2024-03-06T19:18:54Z |
| format | Journal article |
| id | oxford-uuid:195f930c-fba7-405b-879e-6b99bb66eeec |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T19:18:54Z |
| publishDate | 2007 |
| record_format | dspace |
| spelling | oxford-uuid:195f930c-fba7-405b-879e-6b99bb66eeec2022-03-26T10:48:39ZThe solution and crystal structures of a module pair from the Staphylococcus aureus-binding site of human fibronectin--a tale with a twist.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:195f930c-fba7-405b-879e-6b99bb66eeecEnglishSymplectic Elements at Oxford2007Rudiño-Piñera, ERavelli, RSheldrick, GNanao, MKorostelev, VWerner, JSchwarz-Linek, UPotts, JRGarman, EAn 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 (2)F1(3)F1 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 (4)F1(5)F1 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. |
| spellingShingle | Rudiño-Piñera, E Ravelli, R Sheldrick, G Nanao, M Korostelev, V Werner, J Schwarz-Linek, U Potts, JR Garman, E The solution and crystal structures of a module pair from the Staphylococcus aureus-binding site of human fibronectin--a tale with a twist. |
| title | The solution and crystal structures of a module pair from the Staphylococcus aureus-binding site of human fibronectin--a tale with a twist. |
| title_full | The solution and crystal structures of a module pair from the Staphylococcus aureus-binding site of human fibronectin--a tale with a twist. |
| title_fullStr | The solution and crystal structures of a module pair from the Staphylococcus aureus-binding site of human fibronectin--a tale with a twist. |
| title_full_unstemmed | The solution and crystal structures of a module pair from the Staphylococcus aureus-binding site of human fibronectin--a tale with a twist. |
| title_short | The solution and crystal structures of a module pair from the Staphylococcus aureus-binding site of human fibronectin--a tale with a twist. |
| title_sort | solution and crystal structures of a module pair from the staphylococcus aureus binding site of human fibronectin a tale with a twist |
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