High-resolution crystal structure of human Dim2/TXNL4B

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Mar 1;69(Pt 3):223-7. doi: 10.1107/S1744309113000973. Epub 2013 Feb 22.

Abstract

TXNL4A (thioredoxin-like 4A) is an essential protein conserved from yeast to humans and is a component of the pre-mRNA splicing machinery. TXNL4B was identified as a TXNL4-family protein that also interacts with Prp6, an integral component of the U4/U6·U5 tri-snRNP complex, and has been shown to function in pre-mRNA splicing. A crystal structure of TXNL4B was determined at 1.33 Å resolution and refined to an Rwork of 0.13 and an Rfree of 0.18 with one native dimer in the asymmetric unit. Residues 1-33 of TXNL4B have previously been reported to be responsible for its interaction with Prp6. However, this region extends to the β-sheet core of the thioredoxin-fold structure of TXNL4B. This suggests that the interpretation of the previously reported GST pull-down results without considering the structure and stability of TXNL4B is debatable.

Keywords: Dim2; TXNL4B; U5-15kD; human Dim1; pre-mRNA splicing.

MeSH terms

  • Amino Acid Sequence
  • Cell Cycle Proteins / chemistry*
  • Cell Cycle Proteins / genetics
  • Crystallography, X-Ray
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Nuclear Proteins / chemistry*
  • Nuclear Proteins / genetics
  • Protein Multimerization
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Ribonucleoprotein, U5 Small Nuclear / chemistry*
  • Ribonucleoprotein, U5 Small Nuclear / genetics
  • Sequence Alignment
  • Sequence Homology, Amino Acid

Substances

  • Cell Cycle Proteins
  • Nuclear Proteins
  • Recombinant Proteins
  • Ribonucleoprotein, U5 Small Nuclear
  • TXNL4A protein, human
  • TXNL4B protein, human

Associated data

  • PDB/4IN0