Cloning, expression, purification, crystallization and preliminary X-ray studies of the C-terminal domain of Rv3262 (FbiB) from Mycobacterium tuberculosis
During cofactor F420 biosynthesis, the enzyme F420-[gamma]-glutamyl ligase (FbiB) catalyzes the addition of [gamma]-linked L-glutamate residues to form polyglutamylated F420 derivatives. In Mycobacterium tuberculosis, Rv3262 (FbiB) consists of two domains: an N-terminal domain from the F420 ligase s...
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Wiley-Blackwell Publishing, Inc.
2011
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| Online Access: | http://irep.iium.edu.my/9893/ http://irep.iium.edu.my/9893/4/CLONING%2CEXPRESSION%2C_PURIFICATION%2C_CRYSTALLIZATION_AND_PRELIMINARY_X-RAY_STUDIES_OF_THE_C-TERMINAL.pdf |
| _version_ | 1848777167953985536 |
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| author | Mohamed Rehan, Aisyah Paterson, Neil G. Baker, Edward N. Squire, Christopher J. |
| author_facet | Mohamed Rehan, Aisyah Paterson, Neil G. Baker, Edward N. Squire, Christopher J. |
| author_sort | Mohamed Rehan, Aisyah |
| building | IIUM Repository |
| collection | Online Access |
| description | During cofactor F420 biosynthesis, the enzyme F420-[gamma]-glutamyl ligase (FbiB) catalyzes the addition of [gamma]-linked L-glutamate residues to form polyglutamylated F420 derivatives. In Mycobacterium tuberculosis, Rv3262 (FbiB) consists of two domains: an N-terminal domain from the F420 ligase superfamily and a C-terminal domain with sequence similarity to nitro-FMN reductase superfamily proteins. To characterize the role of the C-terminal domain of FbiB in polyglutamyl ligation, it has been purified and crystallized in an apo form. The crystals diffracted to 2.0 Å resolution using a synchrotron source and belonged to the tetragonal space group P41212 (or P43212), with unit-cell parameters a = b = 136.6, c = 101.7 Å, [alpha] = [beta] = [gamma] = 90°. |
| first_indexed | 2025-11-14T14:41:41Z |
| format | Article |
| id | iium-9893 |
| institution | International Islamic University Malaysia |
| institution_category | Local University |
| language | English |
| last_indexed | 2025-11-14T14:41:41Z |
| publishDate | 2011 |
| publisher | Wiley-Blackwell Publishing, Inc. |
| recordtype | eprints |
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| spelling | iium-98932013-06-25T01:51:32Z http://irep.iium.edu.my/9893/ Cloning, expression, purification, crystallization and preliminary X-ray studies of the C-terminal domain of Rv3262 (FbiB) from Mycobacterium tuberculosis Mohamed Rehan, Aisyah Paterson, Neil G. Baker, Edward N. Squire, Christopher J. Q Science (General) QH301 Biology During cofactor F420 biosynthesis, the enzyme F420-[gamma]-glutamyl ligase (FbiB) catalyzes the addition of [gamma]-linked L-glutamate residues to form polyglutamylated F420 derivatives. In Mycobacterium tuberculosis, Rv3262 (FbiB) consists of two domains: an N-terminal domain from the F420 ligase superfamily and a C-terminal domain with sequence similarity to nitro-FMN reductase superfamily proteins. To characterize the role of the C-terminal domain of FbiB in polyglutamyl ligation, it has been purified and crystallized in an apo form. The crystals diffracted to 2.0 Å resolution using a synchrotron source and belonged to the tetragonal space group P41212 (or P43212), with unit-cell parameters a = b = 136.6, c = 101.7 Å, [alpha] = [beta] = [gamma] = 90°. Wiley-Blackwell Publishing, Inc. 2011-10 Article PeerReviewed application/pdf en http://irep.iium.edu.my/9893/4/CLONING%2CEXPRESSION%2C_PURIFICATION%2C_CRYSTALLIZATION_AND_PRELIMINARY_X-RAY_STUDIES_OF_THE_C-TERMINAL.pdf Mohamed Rehan, Aisyah and Paterson, Neil G. and Baker, Edward N. and Squire, Christopher J. (2011) Cloning, expression, purification, crystallization and preliminary X-ray studies of the C-terminal domain of Rv3262 (FbiB) from Mycobacterium tuberculosis. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 67 (10). pp. 1274-1277. ISSN 1744-3091 http://scripts.iucr.org/cgi-bin/paper?S1744309111028958 10.1107/S1744309111028958 |
| spellingShingle | Q Science (General) QH301 Biology Mohamed Rehan, Aisyah Paterson, Neil G. Baker, Edward N. Squire, Christopher J. Cloning, expression, purification, crystallization and preliminary X-ray studies of the C-terminal domain of Rv3262 (FbiB) from Mycobacterium tuberculosis |
| title | Cloning, expression, purification, crystallization
and preliminary X-ray studies of the C-terminal
domain of Rv3262 (FbiB) from Mycobacterium
tuberculosis |
| title_full | Cloning, expression, purification, crystallization
and preliminary X-ray studies of the C-terminal
domain of Rv3262 (FbiB) from Mycobacterium
tuberculosis |
| title_fullStr | Cloning, expression, purification, crystallization
and preliminary X-ray studies of the C-terminal
domain of Rv3262 (FbiB) from Mycobacterium
tuberculosis |
| title_full_unstemmed | Cloning, expression, purification, crystallization
and preliminary X-ray studies of the C-terminal
domain of Rv3262 (FbiB) from Mycobacterium
tuberculosis |
| title_short | Cloning, expression, purification, crystallization
and preliminary X-ray studies of the C-terminal
domain of Rv3262 (FbiB) from Mycobacterium
tuberculosis |
| title_sort | cloning, expression, purification, crystallization
and preliminary x-ray studies of the c-terminal
domain of rv3262 (fbib) from mycobacterium
tuberculosis |
| topic | Q Science (General) QH301 Biology |
| url | http://irep.iium.edu.my/9893/ http://irep.iium.edu.my/9893/ http://irep.iium.edu.my/9893/ http://irep.iium.edu.my/9893/4/CLONING%2CEXPRESSION%2C_PURIFICATION%2C_CRYSTALLIZATION_AND_PRELIMINARY_X-RAY_STUDIES_OF_THE_C-TERMINAL.pdf |