Elongation of the poly-γ-glutamate tail of F420 requires both domains of the F420:γ-glutamyl ligase (FbiB) of Mycobacterium tuberculosis

Elongation of the poly-γ-glutamate tail of F420 requires both domains of the F420:γ-glutamyl ligase (FbiB) of Mycobacterium tuberculosis

Cofactor F420 is an electron carrier with a major role in the oxidoreductive reactions of Mycobacterium tuberculosis (Mtb), the causative agent of tuberculosis (TB). A γ-glutamyl ligase catalyzes the final steps of the F420 biosynthesis pathway by successive additions of L-glutamate residues to F420...

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Main Authors: Bashiri, Ghader, Mohamed Rehan, Aisyah, Sreebhavan, Sreevalsan, Baker, Heather M., Baker, Edward N., Squire, Christopher J.
Format: Article
Language:English
English
Published: American Society for Biochemistry and Molecular Biology Inc. 2016
Subjects:
Q Science (General)
Online Access:http://irep.iium.edu.my/50126/
http://irep.iium.edu.my/50126/
http://irep.iium.edu.my/50126/
http://irep.iium.edu.my/50126/7/50126-Elongation%20of%20the%20poly-%CE%B3-glutamate%20tail%20of.pdf
http://irep.iium.edu.my/50126/4/50126-Elongation_of_the_poly_WOS.pdf
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spelling iium-501262017-10-23T03:37:36Z http://irep.iium.edu.my/50126/ Elongation of the poly-γ-glutamate tail of F420 requires both domains of the F420:γ-glutamyl ligase (FbiB) of Mycobacterium tuberculosis Bashiri, Ghader Mohamed Rehan, Aisyah Sreebhavan, Sreevalsan Baker, Heather M. Baker, Edward N. Squire, Christopher J. Q Science (General) Cofactor F420 is an electron carrier with a major role in the oxidoreductive reactions of Mycobacterium tuberculosis (Mtb), the causative agent of tuberculosis (TB). A γ-glutamyl ligase catalyzes the final steps of the F420 biosynthesis pathway by successive additions of L-glutamate residues to F420-0, producing a poly-γ-glutamate tail. The enzyme responsible for this reaction in Archaea (CofE) comprises a single domain and produces F420-2 as the major species. The homologous Mtb enzyme, FbiB, is a two-domain protein and produces F420 with predominantly 5-7 L-glutamate residues in the poly-γ-glutamate tail. The N-terminal domain of FbiB is homologous to CofE with an annotated γ-glutamyl ligase activity, whereas the C-terminal domain has sequence similarity to an FMN-dependent family of nitroreductase enzymes. Here we demonstrate that full-length FbiB adds multiple L-glutamate residues to F420-0 in vitro to produce F420-5 after 24 hours; communication between the two domains is critical for full γ-glutamyl ligase activity. We also present crystal structures of the C-terminal domain of FbiB in apo, F420-0 and FMN bound states, displaying distinct sites for F420-0 and FMN ligands that partially overlap. Finally, we discuss the features of a full-length structural model produced by small angle X-ray scattering (SAXS) and its implications for the role of N- and C-terminal domains in catalysis. American Society for Biochemistry and Molecular Biology Inc. 2016-03-25 Article PeerReviewed application/pdf en http://irep.iium.edu.my/50126/7/50126-Elongation%20of%20the%20poly-%CE%B3-glutamate%20tail%20of.pdf application/pdf en http://irep.iium.edu.my/50126/4/50126-Elongation_of_the_poly_WOS.pdf Bashiri, Ghader and Mohamed Rehan, Aisyah and Sreebhavan, Sreevalsan and Baker, Heather M. and Baker, Edward N. and Squire, Christopher J. (2016) Elongation of the poly-γ-glutamate tail of F420 requires both domains of the F420:γ-glutamyl ligase (FbiB) of Mycobacterium tuberculosis. Journal of Biological Chemistry, 291 (13). pp. 6882-6894. ISSN 0021-9258 E-ISSN 1083-351X http://www.jbc.org/content/291/13/6882.abstract 10.1074/jbc.M115.689026
repository_type Digital Repository
institution_category Local University
institution International Islamic University Malaysia
building IIUM Repository
collection Online Access
language English
English
topic Q Science (General)
spellingShingle Q Science (General)
Bashiri, Ghader
Mohamed Rehan, Aisyah
Sreebhavan, Sreevalsan
Baker, Heather M.
Baker, Edward N.
Squire, Christopher J.
Elongation of the poly-γ-glutamate tail of F420 requires both domains of the F420:γ-glutamyl ligase (FbiB) of Mycobacterium tuberculosis
description Cofactor F420 is an electron carrier with a major role in the oxidoreductive reactions of Mycobacterium tuberculosis (Mtb), the causative agent of tuberculosis (TB). A γ-glutamyl ligase catalyzes the final steps of the F420 biosynthesis pathway by successive additions of L-glutamate residues to F420-0, producing a poly-γ-glutamate tail. The enzyme responsible for this reaction in Archaea (CofE) comprises a single domain and produces F420-2 as the major species. The homologous Mtb enzyme, FbiB, is a two-domain protein and produces F420 with predominantly 5-7 L-glutamate residues in the poly-γ-glutamate tail. The N-terminal domain of FbiB is homologous to CofE with an annotated γ-glutamyl ligase activity, whereas the C-terminal domain has sequence similarity to an FMN-dependent family of nitroreductase enzymes. Here we demonstrate that full-length FbiB adds multiple L-glutamate residues to F420-0 in vitro to produce F420-5 after 24 hours; communication between the two domains is critical for full γ-glutamyl ligase activity. We also present crystal structures of the C-terminal domain of FbiB in apo, F420-0 and FMN bound states, displaying distinct sites for F420-0 and FMN ligands that partially overlap. Finally, we discuss the features of a full-length structural model produced by small angle X-ray scattering (SAXS) and its implications for the role of N- and C-terminal domains in catalysis.
format Article
author Bashiri, Ghader
Mohamed Rehan, Aisyah
Sreebhavan, Sreevalsan
Baker, Heather M.
Baker, Edward N.
Squire, Christopher J.
author_facet Bashiri, Ghader
Mohamed Rehan, Aisyah
Sreebhavan, Sreevalsan
Baker, Heather M.
Baker, Edward N.
Squire, Christopher J.
author_sort Bashiri, Ghader
title Elongation of the poly-γ-glutamate tail of F420 requires both domains of the F420:γ-glutamyl ligase (FbiB) of Mycobacterium tuberculosis
title_short Elongation of the poly-γ-glutamate tail of F420 requires both domains of the F420:γ-glutamyl ligase (FbiB) of Mycobacterium tuberculosis
title_full Elongation of the poly-γ-glutamate tail of F420 requires both domains of the F420:γ-glutamyl ligase (FbiB) of Mycobacterium tuberculosis
title_fullStr Elongation of the poly-γ-glutamate tail of F420 requires both domains of the F420:γ-glutamyl ligase (FbiB) of Mycobacterium tuberculosis
title_full_unstemmed Elongation of the poly-γ-glutamate tail of F420 requires both domains of the F420:γ-glutamyl ligase (FbiB) of Mycobacterium tuberculosis
title_sort elongation of the poly-γ-glutamate tail of f420 requires both domains of the f420:γ-glutamyl ligase (fbib) of mycobacterium tuberculosis
publisher American Society for Biochemistry and Molecular Biology Inc.
publishDate 2016
url http://irep.iium.edu.my/50126/
http://irep.iium.edu.my/50126/
http://irep.iium.edu.my/50126/
http://irep.iium.edu.my/50126/7/50126-Elongation%20of%20the%20poly-%CE%B3-glutamate%20tail%20of.pdf
http://irep.iium.edu.my/50126/4/50126-Elongation_of_the_poly_WOS.pdf
first_indexed 2023-09-18T21:10:50Z
last_indexed 2023-09-18T21:10:50Z
_version_ 1777411241056141312

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