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The crystal structure of Rv2991 from Mycobacterium tuberculosis: An F 420 binding protein with unknown function
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| 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 |
Abstract
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.
- F, FDOR, Mycobacterium tuberculosis, Structural genomics, Unknown function
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