dc.contributor.author |
Bashiri, Ghader |
en |
dc.contributor.author |
Rehan, AM |
en |
dc.contributor.author |
Sreebhavan, S |
en |
dc.contributor.author |
Baker, Heather |
en |
dc.contributor.author |
Baker, Edward |
en |
dc.contributor.author |
Squire, Christopher |
en |
dc.date.accessioned |
2016-08-05T00:03:37Z |
en |
dc.date.issued |
2016-03-25 |
en |
dc.identifier.citation |
Journal of Biological Chemistry, 2016, 291 (13), pp. 6882 - 6894 |
en |
dc.identifier.issn |
0021-9258 |
en |
dc.identifier.uri |
http://hdl.handle.net/2292/29806 |
en |
dc.description.abstract |
Cofactor F420is an electron carrier with a major role in the oxidoreductive reactions ofMycobacterium tuberculosis, the causative agent of tuberculosis. A γ-glutamyl ligase catalyzes the final steps of the F420biosynthesis pathway by successive additions ofl-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 homologousM. tuberculosisenzyme, FbiB, is a two-domain protein and produces F420with predominantly 5-7l-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 multiplel-glutamate residues to F420-0in vitroto produce F420-5 after 24 h; 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 and its implications for the role of N- and C-terminal domains in catalysis. |
en |
dc.description.uri |
http://www.jbc.org/ |
en |
dc.publisher |
American Society for Biochemistry and Molecular Biology |
en |
dc.relation.ispartofseries |
Journal of Biological Chemistry |
en |
dc.rights |
Items in ResearchSpace are protected by copyright, with all rights reserved, unless otherwise indicated. Previously published items are made available in accordance with the copyright policy of the publisher. Details obtained from http://www.sherpa.ac.uk/romeo/issn/0021-9258/ |
en |
dc.rights.uri |
https://researchspace.auckland.ac.nz/docs/uoa-docs/rights.htm |
en |
dc.title |
Elongation of the Poly-γ-glutamate Tail of F420 Requires Both Domains of the F420:γ-Glutamyl Ligase (FbiB) of Mycobacterium tuberculosis |
en |
dc.type |
Journal Article |
en |
dc.identifier.doi |
10.1074/jbc.M115.689026 |
en |
pubs.issue |
13 |
en |
pubs.begin-page |
6882 |
en |
pubs.volume |
291 |
en |
dc.description.version |
VoR – Version of Record |
en |
dc.rights.holder |
Copyright:
American Society for Biochemistry and Molecular Biology |
en |
dc.identifier.pmid |
26861878 |
en |
pubs.author-url |
http://www.jbc.org/content/291/13/6882.full |
en |
pubs.end-page |
6894 |
en |
pubs.publication-status |
Published |
en |
dc.rights.accessrights |
http://purl.org/eprint/accessRights/OpenAccess |
en |
pubs.subtype |
Article |
en |
pubs.elements-id |
522900 |
en |
pubs.org-id |
Science |
en |
pubs.org-id |
Biological Sciences |
en |
pubs.org-id |
Science Research |
en |
pubs.org-id |
Maurice Wilkins Centre (2010-2014) |
en |
dc.identifier.eissn |
1083-351X |
en |
pubs.record-created-at-source-date |
2016-08-05 |
en |
pubs.dimensions-id |
26861878 |
en |