Benini, Stefano, Haouz, Ahmed, Proux, Florence et al. (2 more authors) (2019) The crystal structure of Rv2991 from Mycobacterium tuberculosis:An F 420 binding protein with unknown function. JOURNAL OF STRUCTURAL BIOLOGY. pp. 216-224. ISSN 1047-8477
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.
Metadata
Item Type: | Article |
---|---|
Authors/Creators: |
|
Keywords: | F,FDOR,Mycobacterium tuberculosis,Structural genomics,Unknown function |
Dates: |
|
Institution: | The University of York |
Academic Units: | The University of York > Faculty of Sciences (York) > Chemistry (York) |
Depositing User: | Pure (York) |
Date Deposited: | 20 Jun 2019 14:00 |
Last Modified: | 26 Jan 2025 00:14 |
Published Version: | https://doi.org/10.1016/j.jsb.2019.03.006 |
Status: | Published |
Refereed: | Yes |
Identification Number: | 10.1016/j.jsb.2019.03.006 |
Related URLs: | |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:147627 |