By the same authors

From the same journal

From the same journal

The crystal structure of Rv2991 from Mycobacterium tuberculosis: An F 420 binding protein with unknown function

Research output: Contribution to journalArticle

Published copy (DOI)

Author(s)

  • Stefano Benini
  • Ahmed Haouz
  • Florence Proux
  • Pedro Alzari
  • Keith Wilson

Department/unit(s)

Publication details

JournalJOURNAL OF STRUCTURAL BIOLOGY
DateAccepted/In press - 14 Mar 2019
DateE-pub ahead of print - 16 Mar 2019
DatePublished (current) - 1 May 2019
Issue number2
Volume206
Number of pages9
Pages (from-to)216-224
Early online date16/03/19
Original languageEnglish

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.

    Research areas

  • F, FDOR, Mycobacterium tuberculosis, Structural genomics, Unknown function

Discover related content

Find related publications, people, projects, datasets and more using interactive charts.

View graph of relations