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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: Mohamed Rehan, Aisyah
Format: Conference or Workshop Item
Language:English
Published: 2009
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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spelling my.iium.irep.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 REM 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)
institution Universiti Islam Antarabangsa Malaysia
building IIUM Library
collection Institutional Repository
continent Asia
country Malaysia
content_provider International Islamic University Malaysia
content_source IIUM Repository (IREP)
url_provider http://irep.iium.edu.my/
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/12423/1/Structure_and_Function_of_Proteins_in_Mycobacterium_tuberculosis_Energy_Metabolism.pdf
http://irep.iium.edu.my/12423/
_version_ 1643606619634794496
score 13.211869

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