Structure of the cold-shock domain protein from Neisseria meningitidis reveals a strand-exchanged dimer.
The structure of the cold-shock domain protein from Neisseria meningitidis has been solved to 2.6 A resolution and shown to comprise a dimer formed by the exchange of two beta-strands between protein monomers. The overall fold of the monomer closely resembles those of other bacterial cold-shock prot...
| Autors principals: | , , , , |
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| Format: | Journal article |
| Idioma: | English |
| Publicat: |
2008
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| _version_ | 1826270553472761856 |
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| author | Ren, J Nettleship, J Sainsbury, S Saunders, N Owens, R |
| author_facet | Ren, J Nettleship, J Sainsbury, S Saunders, N Owens, R |
| author_sort | Ren, J |
| collection | OXFORD |
| description | The structure of the cold-shock domain protein from Neisseria meningitidis has been solved to 2.6 A resolution and shown to comprise a dimer formed by the exchange of two beta-strands between protein monomers. The overall fold of the monomer closely resembles those of other bacterial cold-shock proteins. The neisserial protein behaved as a monomer in solution and was shown to bind to a hexathymidine oligonucleotide with a stoichiometry of 1:1 and a K(d) of 1.25 microM. |
| first_indexed | 2024-03-06T21:42:38Z |
| format | Journal article |
| id | oxford-uuid:4873665a-d5d0-48a5-a66a-f81ec18d56f3 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T21:42:38Z |
| publishDate | 2008 |
| record_format | dspace |
| spelling | oxford-uuid:4873665a-d5d0-48a5-a66a-f81ec18d56f32022-03-26T15:25:55ZStructure of the cold-shock domain protein from Neisseria meningitidis reveals a strand-exchanged dimer.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:4873665a-d5d0-48a5-a66a-f81ec18d56f3EnglishSymplectic Elements at Oxford2008Ren, JNettleship, JSainsbury, SSaunders, NOwens, RThe structure of the cold-shock domain protein from Neisseria meningitidis has been solved to 2.6 A resolution and shown to comprise a dimer formed by the exchange of two beta-strands between protein monomers. The overall fold of the monomer closely resembles those of other bacterial cold-shock proteins. The neisserial protein behaved as a monomer in solution and was shown to bind to a hexathymidine oligonucleotide with a stoichiometry of 1:1 and a K(d) of 1.25 microM. |
| spellingShingle | Ren, J Nettleship, J Sainsbury, S Saunders, N Owens, R Structure of the cold-shock domain protein from Neisseria meningitidis reveals a strand-exchanged dimer. |
| title | Structure of the cold-shock domain protein from Neisseria meningitidis reveals a strand-exchanged dimer. |
| title_full | Structure of the cold-shock domain protein from Neisseria meningitidis reveals a strand-exchanged dimer. |
| title_fullStr | Structure of the cold-shock domain protein from Neisseria meningitidis reveals a strand-exchanged dimer. |
| title_full_unstemmed | Structure of the cold-shock domain protein from Neisseria meningitidis reveals a strand-exchanged dimer. |
| title_short | Structure of the cold-shock domain protein from Neisseria meningitidis reveals a strand-exchanged dimer. |
| title_sort | structure of the cold shock domain protein from neisseria meningitidis reveals a strand exchanged dimer |
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