1.9 Å resolution crystal structure of the Saccharomyces cerevisiae Ran-binding protein Mog1p

Murray Stewart, Rosanna Baker

Research output: Contribution to journalArticle

Abstract

The 1.9 Å resolution X-ray crystal structure of Ran-binding protein Mog1p shows that it has a unique fold based on a six-stranded antiparallel β-sheet backed on both sides by an extensive α-helix. The topology of some elements of Mog1p secondary structure resemble a portion of nuclear transport factor 2 (NTF2), but the hydrophobic cavity and surrounding negatively charged residues that are important in the NTF2-RanGDP interaction are not conserved in Mog1p. In addition to binding RanGTP, Mog1p forms a 1:1 complex with RanGDP and so binds Ran independent of its nucleotide state. Mog1p and NTF2 compete for binding to RanGDP indicating that their binding sites on RanGDP are sufficiently close to prevent both proteins binding simultaneously. Although there may be some overlap between the Mog1p and NTF2 binding sites on RanGDP, these sites are not identical. Sequence analysis of Mog1p homologues from Schizosaccharomyces pombe, human, and Caenorhabditis elegans in the context of the Mog1p crystal structure indicates the presence of a cluster of highly conserved surface residues consistent with an interaction site for Ran. (C) 2000 Academic Press.

Original languageEnglish (US)
Pages (from-to)213-223
Number of pages11
JournalJournal of Molecular Biology
Volume299
Issue number1
DOIs
StatePublished - May 26 2000
Externally publishedYes

Fingerprint

ran GTP-Binding Protein
Saccharomyces cerevisiae Proteins
Cell Nucleus Active Transport
Carrier Proteins
Binding Sites
Schizosaccharomyces
Caenorhabditis elegans
Protein Binding
Sequence Analysis
Nucleotides
X-Rays

Keywords

  • Binding site
  • GTPase
  • NTF2
  • Nuclear trafficking

ASJC Scopus subject areas

  • Virology

Cite this

1.9 Å resolution crystal structure of the Saccharomyces cerevisiae Ran-binding protein Mog1p. / Stewart, Murray; Baker, Rosanna.

In: Journal of Molecular Biology, Vol. 299, No. 1, 26.05.2000, p. 213-223.

Research output: Contribution to journalArticle

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