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/ 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 |
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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 |
| repository_type |
Digital Repository |
| institution_category |
Local University |
| institution |
International Islamic University Malaysia |
| building |
IIUM Repository |
| collection |
Online Access |
| language |
English |
| topic |
Q Science (General) QH301 Biology |
| 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 |
| 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°. |
| format |
Article |
| 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 |
| title |
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_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_sort |
cloning, expression, purification, crystallization
and preliminary x-ray studies of the c-terminal
domain of rv3262 (fbib) from mycobacterium
tuberculosis |
| publisher |
Wiley-Blackwell Publishing, Inc. |
| publishDate |
2011 |
| 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 |
| first_indexed |
2023-09-18T20:19:29Z |
| last_indexed |
2023-09-18T20:19:29Z |
| _version_ |
1777408010144972800 |