Structure and function of proteins important in Mycobacterium tuberculosis energy metabolism
Mycobacterium tuberculosis (Mb) is the causative agent of tuberculosis (TB). A unique feature of Mtb is that it can remain dormant within the human host for years (persistance), and can survive in hypoxic and nutrient-depleted media. Coenzyme F420, a flavin analogue has been hypothesized to be assoc...
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2009
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| Online Access: | http://irep.iium.edu.my/12423/ http://irep.iium.edu.my/12423/1/Structure_and_Function_of_Proteins_in_Mycobacterium_tuberculosis_Energy_Metabolism.pdf |
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iium-124232012-01-12T04:35:05Z http://irep.iium.edu.my/12423/ Structure and function of proteins important in Mycobacterium tuberculosis energy metabolism Mohamed Rehan, Aisyah Mycobacterium tuberculosis (Mb) is the causative agent of tuberculosis (TB). A unique feature of Mtb is that it can remain dormant within the human host for years (persistance), and can survive in hypoxic and nutrient-depleted media. Coenzyme F420, a flavin analogue has been hypothesized to be associated with Mtb viability in anaerobic conditions and in persistence. This hydride carrier also acts as a redox sensor in Mtb by converting NO2 to NO released by Mtb-infected macrophages under aerobic condition. At least three genes are involved in the biosynthesis of F420; F420 biosynthesis A, B and C (fbiA, fbiB and fbiC). This PhD project will explore F420 biosynthesis using biophysical techniques. The fbiA and fbiB genes were cloned in a pET-Duet vector to test for protein interaction. While co-expression was unsuccessful, single expression of the genes produced soluble protein. FbiB has been purified and crystallized as small needles. Purification of a GST-tagged construct to eliminate proteolytic degradation and further fine screening is ongoing to obtain better quality crystals for X-ray diffraction. FbiC cloning into Gateway vectors is ongoing. Further biochemical and biophysical tests hopefully obtained in the near future will assist in our understanding of this unique coenzyme. 2009 Conference or Workshop Item NonPeerReviewed application/pdf en http://irep.iium.edu.my/12423/1/Structure_and_Function_of_Proteins_in_Mycobacterium_tuberculosis_Energy_Metabolism.pdf Mohamed Rehan, Aisyah (2009) Structure and function of proteins important in Mycobacterium tuberculosis energy metabolism. In: Roche First Year PhD Seminar Day, organised by School of Biological Sciences, The University of Auckland, 9 June 2009, The University of Auckland, Auckland, New Zealand. (Unpublished) |
| repository_type |
Digital Repository |
| institution_category |
Local University |
| institution |
International Islamic University Malaysia |
| building |
IIUM Repository |
| collection |
Online Access |
| language |
English |
| description |
Mycobacterium tuberculosis (Mb) is the causative agent of tuberculosis (TB). A unique feature of Mtb is that it can remain dormant within the human host for years (persistance), and can survive in hypoxic and nutrient-depleted media. Coenzyme F420, a flavin analogue has been hypothesized to be associated with Mtb viability in anaerobic conditions and in persistence. This hydride carrier also acts as a redox sensor in Mtb by converting NO2 to NO released by Mtb-infected macrophages under aerobic condition. At least three genes are involved in the biosynthesis of F420; F420 biosynthesis A, B and C (fbiA, fbiB and fbiC). This PhD project will explore F420 biosynthesis using biophysical techniques. The fbiA and fbiB genes were cloned in a pET-Duet vector to test for protein interaction. While co-expression was unsuccessful, single expression of the genes produced soluble protein. FbiB has been purified and crystallized as small needles. Purification of a GST-tagged construct to eliminate proteolytic degradation and further fine screening is ongoing to obtain better quality crystals for X-ray diffraction. FbiC cloning into Gateway vectors is ongoing. Further biochemical and biophysical tests hopefully obtained in the near future will assist in our understanding of this unique coenzyme. |
| format |
Conference or Workshop Item |
| author |
Mohamed Rehan, Aisyah |
| spellingShingle |
Mohamed Rehan, Aisyah Structure and function of proteins important in Mycobacterium tuberculosis energy metabolism |
| author_facet |
Mohamed Rehan, Aisyah |
| author_sort |
Mohamed Rehan, Aisyah |
| title |
Structure and function of proteins important in Mycobacterium tuberculosis energy metabolism |
| title_short |
Structure and function of proteins important in Mycobacterium tuberculosis energy metabolism |
| title_full |
Structure and function of proteins important in Mycobacterium tuberculosis energy metabolism |
| title_fullStr |
Structure and function of proteins important in Mycobacterium tuberculosis energy metabolism |
| title_full_unstemmed |
Structure and function of proteins important in Mycobacterium tuberculosis energy metabolism |
| title_sort |
structure and function of proteins important in mycobacterium tuberculosis energy metabolism |
| publishDate |
2009 |
| url |
http://irep.iium.edu.my/12423/ http://irep.iium.edu.my/12423/1/Structure_and_Function_of_Proteins_in_Mycobacterium_tuberculosis_Energy_Metabolism.pdf |
| first_indexed |
2023-09-18T20:21:38Z |
| last_indexed |
2023-09-18T20:21:38Z |
| _version_ |
1777408145995333632 |