Crystallization and X-ray diffraction analysis of the DNA-remodelling protein DnaD from Bacillus subtilis.
The DnaD protein is an essential component of the chromosome-replication machinery of the Gram-positive bacterium Bacillus subtilis and is part of the primosomal cascade that ultimately loads the replicative ring helicase DnaC onto DNA. Moreover, DnaD is a global regulator of DNA architecture, as it...
| Main Authors: | , , , , |
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| Format: | Journal article |
| Language: | English |
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2007
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| _version_ | 1797054404988239872 |
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| author | Schneider, S Carneiro, M Ioannou, C Soultanas, P Paoli, M |
| author_facet | Schneider, S Carneiro, M Ioannou, C Soultanas, P Paoli, M |
| author_sort | Schneider, S |
| collection | OXFORD |
| description | The DnaD protein is an essential component of the chromosome-replication machinery of the Gram-positive bacterium Bacillus subtilis and is part of the primosomal cascade that ultimately loads the replicative ring helicase DnaC onto DNA. Moreover, DnaD is a global regulator of DNA architecture, as it forms higher order nucleoprotein structures in order to open supercoiled DNA. Here, the crystallization and preliminary X-ray diffraction analysis of the two domains of DnaD from B. subtilis are reported. Crystals of the N-terminal domain are trigonal, with either P3(1)21 or P3(2)21 space-group symmetry, and diffracted X-rays to 2.0 A resolution; crystals of the C-terminal domain are hexagonal, with space group P6(1) or P6(5), and diffracted X-rays to 2.9 A resolution in-house. Determination of the structure of the DnaD domains will provide insight into how remodelling of the nucleoid is associated with priming of replication in the model Gram-positive organism B. subtilis. |
| first_indexed | 2024-03-06T18:56:49Z |
| format | Journal article |
| id | oxford-uuid:121d4a11-cb8d-4dda-b78b-e9b126d60306 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T18:56:49Z |
| publishDate | 2007 |
| record_format | dspace |
| spelling | oxford-uuid:121d4a11-cb8d-4dda-b78b-e9b126d603062022-03-26T10:06:03ZCrystallization and X-ray diffraction analysis of the DNA-remodelling protein DnaD from Bacillus subtilis.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:121d4a11-cb8d-4dda-b78b-e9b126d60306EnglishSymplectic Elements at Oxford2007Schneider, SCarneiro, MIoannou, CSoultanas, PPaoli, MThe DnaD protein is an essential component of the chromosome-replication machinery of the Gram-positive bacterium Bacillus subtilis and is part of the primosomal cascade that ultimately loads the replicative ring helicase DnaC onto DNA. Moreover, DnaD is a global regulator of DNA architecture, as it forms higher order nucleoprotein structures in order to open supercoiled DNA. Here, the crystallization and preliminary X-ray diffraction analysis of the two domains of DnaD from B. subtilis are reported. Crystals of the N-terminal domain are trigonal, with either P3(1)21 or P3(2)21 space-group symmetry, and diffracted X-rays to 2.0 A resolution; crystals of the C-terminal domain are hexagonal, with space group P6(1) or P6(5), and diffracted X-rays to 2.9 A resolution in-house. Determination of the structure of the DnaD domains will provide insight into how remodelling of the nucleoid is associated with priming of replication in the model Gram-positive organism B. subtilis. |
| spellingShingle | Schneider, S Carneiro, M Ioannou, C Soultanas, P Paoli, M Crystallization and X-ray diffraction analysis of the DNA-remodelling protein DnaD from Bacillus subtilis. |
| title | Crystallization and X-ray diffraction analysis of the DNA-remodelling protein DnaD from Bacillus subtilis. |
| title_full | Crystallization and X-ray diffraction analysis of the DNA-remodelling protein DnaD from Bacillus subtilis. |
| title_fullStr | Crystallization and X-ray diffraction analysis of the DNA-remodelling protein DnaD from Bacillus subtilis. |
| title_full_unstemmed | Crystallization and X-ray diffraction analysis of the DNA-remodelling protein DnaD from Bacillus subtilis. |
| title_short | Crystallization and X-ray diffraction analysis of the DNA-remodelling protein DnaD from Bacillus subtilis. |
| title_sort | crystallization and x ray diffraction analysis of the dna remodelling protein dnad from bacillus subtilis |
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