Research output: Contribution to journal › Article › peer-review
1.59 MB, PDF document
Journal | JOURNAL OF STRUCTURAL BIOLOGY |
---|---|
Date | Accepted/In press - 14 Mar 2019 |
Date | E-pub ahead of print - 16 Mar 2019 |
Date | Published (current) - 1 May 2019 |
Issue number | 2 |
Volume | 206 |
Number of pages | 9 |
Pages (from-to) | 216-224 |
Early online date | 16/03/19 |
Original language | English |
The crystal structure of the conserved hypothetical protein Rv2991 from Mycobacterium tuberculosis has been solved by SAD using seleno-methionine substituted protein. The dimeric biological assembly and the sequence and fold conservation are typical of F 420 cofactor binding enzymes. Despite Rv2991 still being of unknown function, sequence and structural comparison with similar proteins enable a role to be proposed for its C-terminal stretch of residues in recognizing and orienting the substrate. In addition, the C-terminus is involved in both protein folding and determining the size of the active site cavity.
Find related publications, people, projects, datasets and more using interactive charts.