1RFE

Crystal structure of conserved hypothetical protein Rv2991 from Mycobacterium tuberculosis

Summary for 1RFE

• Entry DOI: 10.2210/pdb1rfe/pdb
• Descriptor: hypothetical protein Rv2991 (2 entities in total)
• Functional Keywords: structural genomics, tb, mycobacterium tuberculosis, fmn binding, psi, protein structure initiative, tb structural genomics consortium, tbsgc, unknown function
• Biological source: Mycobacterium tuberculosis
• Total number of polymer chains: 1
• Total formula weight: 18394.85

Authors

Benini, S.,Haouz, A.,Proux, F.,Betton, J.M.,Alzari, P.,Dodson, G.G.,Wilson, K.S.,TB Structural Genomics Consortium (TBSGC) (deposition date: 2003-11-08, release date: 2004-12-28, Last modification date: 2025-03-26)

Primary citation

Benini, S.,Haouz, A.,Proux, F.,Alzari, P.,Wilson, K.
The crystal structure of Rv2991 from Mycobacterium tuberculosis: An F420binding protein with unknown function.
J. Struct. Biol., 2019

PubMed 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 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.

PubMed: 30890426
DOI: 10.1016/j.jsb.2019.03.006

Experimental method

X-RAY DIFFRACTION (2 Å)