The atomic structure of Carnation Mottle Virus capsid protein.
The structure of the Carnation Mottle Virus (CMtV) capsid protein has been determined at 3.2 A resolution by the method of molecular replacement. Three-dimensional data were collected from a small number of crystals (sp.g. I23, a = 382.6 A) using the synchrotron radiation with an image plate as dete...
| Main Authors: | , , , , , , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
1994
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| _version_ | 1797098041023397888 |
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| author | Morgunova EYu Dauter, Z Fry, E Stuart, D Stel'mashchuk VYa Mikhailov, A Wilson, K Vainshtein, B |
| author_facet | Morgunova EYu Dauter, Z Fry, E Stuart, D Stel'mashchuk VYa Mikhailov, A Wilson, K Vainshtein, B |
| author_sort | Morgunova EYu |
| collection | OXFORD |
| description | The structure of the Carnation Mottle Virus (CMtV) capsid protein has been determined at 3.2 A resolution by the method of molecular replacement. Three-dimensional data were collected from a small number of crystals (sp.g. I23, a = 382.6 A) using the synchrotron radiation with an image plate as detector. The coordinates of Tomato Bushy Stunt Virus (TBSV) were used as a searching model. Refinement of the coordinates of 7,479 non-hydrogen atoms performed by the program XPLOR, has led to an R-factor of 18.3%. It was found that the amino acid chain fold of capsid protein is very similar to that in other icosahedral viruses. However, there are some differences in the contact regions between protein subunits and also the lack of the beta-annulus around the 3-fold icosahedral axes. The structural and biochemical results lead us to consider an alternative assembly pathway. |
| first_indexed | 2024-03-07T05:03:58Z |
| format | Journal article |
| id | oxford-uuid:d9477ff8-ec28-4434-8da4-7f2e6bcb9b8c |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T05:03:58Z |
| publishDate | 1994 |
| record_format | dspace |
| spelling | oxford-uuid:d9477ff8-ec28-4434-8da4-7f2e6bcb9b8c2022-03-27T08:54:47ZThe atomic structure of Carnation Mottle Virus capsid protein.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:d9477ff8-ec28-4434-8da4-7f2e6bcb9b8cEnglishSymplectic Elements at Oxford1994Morgunova EYuDauter, ZFry, EStuart, DStel'mashchuk VYaMikhailov, AWilson, KVainshtein, BThe structure of the Carnation Mottle Virus (CMtV) capsid protein has been determined at 3.2 A resolution by the method of molecular replacement. Three-dimensional data were collected from a small number of crystals (sp.g. I23, a = 382.6 A) using the synchrotron radiation with an image plate as detector. The coordinates of Tomato Bushy Stunt Virus (TBSV) were used as a searching model. Refinement of the coordinates of 7,479 non-hydrogen atoms performed by the program XPLOR, has led to an R-factor of 18.3%. It was found that the amino acid chain fold of capsid protein is very similar to that in other icosahedral viruses. However, there are some differences in the contact regions between protein subunits and also the lack of the beta-annulus around the 3-fold icosahedral axes. The structural and biochemical results lead us to consider an alternative assembly pathway. |
| spellingShingle | Morgunova EYu Dauter, Z Fry, E Stuart, D Stel'mashchuk VYa Mikhailov, A Wilson, K Vainshtein, B The atomic structure of Carnation Mottle Virus capsid protein. |
| title | The atomic structure of Carnation Mottle Virus capsid protein. |
| title_full | The atomic structure of Carnation Mottle Virus capsid protein. |
| title_fullStr | The atomic structure of Carnation Mottle Virus capsid protein. |
| title_full_unstemmed | The atomic structure of Carnation Mottle Virus capsid protein. |
| title_short | The atomic structure of Carnation Mottle Virus capsid protein. |
| title_sort | atomic structure of carnation mottle virus capsid protein |
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