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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| Main Author: | |
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| Format: | Conference or Workshop Item |
| Language: | English |
| Published: |
2009
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| Online Access: | http://irep.iium.edu.my/12423/1/Structure_and_Function_of_Proteins_in_Mycobacterium_tuberculosis_Energy_Metabolism.pdf http://irep.iium.edu.my/12423/ |
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| Institution: | Universiti Islam Antarabangsa Malaysia |
| Language: | English |
| Summary: | 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. |
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