Rigidifying acyl carrier protein domain in iterative type I PKS CalE8 does not affect its function
Acyl carrier protein (ACP) domains shuttle acyl intermediates among the catalytic domains of multidomain type I fatty acid synthase and polyketide synthase (PKS) systems. It is believed that the unique function of ACPs is associated with their dynamic property, but it remains to be fully elucidated...
| Главные авторы: | , , , , , , |
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| Другие авторы: | |
| Формат: | Journal Article |
| Язык: | English |
| Опубликовано: |
2013
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| Предметы: | |
| Online-ссылка: | https://hdl.handle.net/10356/96023 http://hdl.handle.net/10220/10787 |
| _version_ | 1826118183347552256 |
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| author | Lim, Jackwee Sun, Huihua Fan, Jing-Song Hameed, Iman Fahim Lescar, Julien Liang, Zhao-Xun Yang, Daiwen |
| author2 | School of Biological Sciences |
| author_facet | School of Biological Sciences Lim, Jackwee Sun, Huihua Fan, Jing-Song Hameed, Iman Fahim Lescar, Julien Liang, Zhao-Xun Yang, Daiwen |
| author_sort | Lim, Jackwee |
| collection | NTU |
| description | Acyl carrier protein (ACP) domains shuttle acyl intermediates among the catalytic domains of multidomain type I fatty acid synthase and polyketide synthase (PKS) systems. It is believed that the unique function of ACPs is associated with their dynamic property, but it remains to be fully elucidated what type of protein dynamics is critical for the shuttling domain. Using NMR techniques, we found that the ACP domain of iterative type I PKS CalE8 from Micromonospora echinospora is highly dynamic on the millisecond-second timescale. Introduction of an interhelical disulfide linkage in the ACP domain suppresses the dynamics on the millisecond-second timescale and reduces the mobility on the picosecond-nanosecond timescale. We demonstrate that the full-length PKS is fully functional upon rigidification of the ACP domain, suggesting that although the flexibility of the disordered terminal linkers may be important for the function of the ACP domain, the internal dynamics of the helical regions is not critical for that function. |
| first_indexed | 2024-10-01T04:39:33Z |
| format | Journal Article |
| id | ntu-10356/96023 |
| institution | Nanyang Technological University |
| language | English |
| last_indexed | 2024-10-01T04:39:33Z |
| publishDate | 2013 |
| record_format | dspace |
| spelling | ntu-10356/960232022-02-16T16:26:41Z Rigidifying acyl carrier protein domain in iterative type I PKS CalE8 does not affect its function Lim, Jackwee Sun, Huihua Fan, Jing-Song Hameed, Iman Fahim Lescar, Julien Liang, Zhao-Xun Yang, Daiwen School of Biological Sciences DRNTU::Science::Biological sciences Acyl carrier protein (ACP) domains shuttle acyl intermediates among the catalytic domains of multidomain type I fatty acid synthase and polyketide synthase (PKS) systems. It is believed that the unique function of ACPs is associated with their dynamic property, but it remains to be fully elucidated what type of protein dynamics is critical for the shuttling domain. Using NMR techniques, we found that the ACP domain of iterative type I PKS CalE8 from Micromonospora echinospora is highly dynamic on the millisecond-second timescale. Introduction of an interhelical disulfide linkage in the ACP domain suppresses the dynamics on the millisecond-second timescale and reduces the mobility on the picosecond-nanosecond timescale. We demonstrate that the full-length PKS is fully functional upon rigidification of the ACP domain, suggesting that although the flexibility of the disordered terminal linkers may be important for the function of the ACP domain, the internal dynamics of the helical regions is not critical for that function. 2013-06-27T04:02:17Z 2019-12-06T19:24:37Z 2013-06-27T04:02:17Z 2019-12-06T19:24:37Z 2012 2012 Journal Article Lim, J., Sun, H., Fan, J.-S., Hameed, I. F., Lescar, J., Liang, Z.-X., et al. (2012). Rigidifying Acyl Carrier Protein Domain in Iterative Type I PKS CalE8 Does Not Affect Its Function. Biophysical Journal, 103(5), 1037-1044. 0006-3495 https://hdl.handle.net/10356/96023 http://hdl.handle.net/10220/10787 10.1016/j.bpj.2012.08.006 23009853 en Biophysical journal © 2012 The Biophysical Society. |
| spellingShingle | DRNTU::Science::Biological sciences Lim, Jackwee Sun, Huihua Fan, Jing-Song Hameed, Iman Fahim Lescar, Julien Liang, Zhao-Xun Yang, Daiwen Rigidifying acyl carrier protein domain in iterative type I PKS CalE8 does not affect its function |
| title | Rigidifying acyl carrier protein domain in iterative type I PKS CalE8 does not affect its function |
| title_full | Rigidifying acyl carrier protein domain in iterative type I PKS CalE8 does not affect its function |
| title_fullStr | Rigidifying acyl carrier protein domain in iterative type I PKS CalE8 does not affect its function |
| title_full_unstemmed | Rigidifying acyl carrier protein domain in iterative type I PKS CalE8 does not affect its function |
| title_short | Rigidifying acyl carrier protein domain in iterative type I PKS CalE8 does not affect its function |
| title_sort | rigidifying acyl carrier protein domain in iterative type i pks cale8 does not affect its function |
| topic | DRNTU::Science::Biological sciences |
| url | https://hdl.handle.net/10356/96023 http://hdl.handle.net/10220/10787 |
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