The bacterial helicase-primase interaction: a common structural/functional module
The lack of a high-resolution structure for the bacterial helicase-primase complex and the fragmented structural information for the individual proteins have been hindering our detailed understanding of this crucial binary protein interaction. Two new structures for the helicase-interacting domain o...
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| Format: | Article |
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Elsevier
2005
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| Online Access: | https://eprints.nottingham.ac.uk/1106/ |
| _version_ | 1848790539226316800 |
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| author | Soultanas, Panos |
| author_facet | Soultanas, Panos |
| author_sort | Soultanas, Panos |
| building | Nottingham Research Data Repository |
| collection | Online Access |
| description | The lack of a high-resolution structure for the bacterial helicase-primase complex and the fragmented structural information for the individual proteins have been hindering our detailed understanding of this crucial binary protein interaction. Two new structures for the helicase-interacting domain of the bacterial primases from Escherichia coli and Bacillus stearothermophilus have recently been solved and both revealed a unique and surprising structural similarity to the amino-terminal domain of the helicase itself. In this minireview, the current data are discussed and important new structural and functional aspects of the helicase-primase interaction are highlighted. An attractive structural model with direct biological significance for the function of this complex and also for the development of new antibacterial compounds is examined. |
| first_indexed | 2025-11-14T18:14:13Z |
| format | Article |
| id | nottingham-1106 |
| institution | University of Nottingham Malaysia Campus |
| institution_category | Local University |
| last_indexed | 2025-11-14T18:14:13Z |
| publishDate | 2005 |
| publisher | Elsevier |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | nottingham-11062020-05-04T20:30:34Z https://eprints.nottingham.ac.uk/1106/ The bacterial helicase-primase interaction: a common structural/functional module Soultanas, Panos The lack of a high-resolution structure for the bacterial helicase-primase complex and the fragmented structural information for the individual proteins have been hindering our detailed understanding of this crucial binary protein interaction. Two new structures for the helicase-interacting domain of the bacterial primases from Escherichia coli and Bacillus stearothermophilus have recently been solved and both revealed a unique and surprising structural similarity to the amino-terminal domain of the helicase itself. In this minireview, the current data are discussed and important new structural and functional aspects of the helicase-primase interaction are highlighted. An attractive structural model with direct biological significance for the function of this complex and also for the development of new antibacterial compounds is examined. Elsevier 2005-06 Article PeerReviewed Soultanas, Panos (2005) The bacterial helicase-primase interaction: a common structural/functional module. Structure, 13 (6). pp. 839-844. ISSN 0969-2126 http://www.elsevier.com/wps/find/journaldescription.cws_home/622315/description#description doi:10.1016/j.str.2005.04.006 doi:10.1016/j.str.2005.04.006 |
| spellingShingle | Soultanas, Panos The bacterial helicase-primase interaction: a common structural/functional module |
| title | The bacterial helicase-primase interaction: a common structural/functional module |
| title_full | The bacterial helicase-primase interaction: a common structural/functional module |
| title_fullStr | The bacterial helicase-primase interaction: a common structural/functional module |
| title_full_unstemmed | The bacterial helicase-primase interaction: a common structural/functional module |
| title_short | The bacterial helicase-primase interaction: a common structural/functional module |
| title_sort | bacterial helicase-primase interaction: a common structural/functional module |
| url | https://eprints.nottingham.ac.uk/1106/ https://eprints.nottingham.ac.uk/1106/ https://eprints.nottingham.ac.uk/1106/ |