1R5O

crystal structure analysis of sup35 complexed with GMPPNP

Summary for 1R5O

• Entry DOI: 10.2210/pdb1r5o/pdb
• Related: 1R5B 1R5N
• Descriptor: Eukaryotic peptide chain release factor GTP-binding subunit, PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER (3 entities in total)
• Functional Keywords: translation termination, peptide release, gtpase, translation
• Biological source: Schizosaccharomyces pombe (fission yeast)
• Cellular location: Cytoplasm (Probable): O74718
• Total number of polymer chains: 1
• Total formula weight: 52625.39

Authors

Kong, C.,Song, H. (deposition date: 2003-10-11, release date: 2004-05-25, Last modification date: 2023-10-25)

Primary citation

Kong, C.,Ito, K.,Walsh, M.A.,Wada, M.,Liu, Y.,Kumar, S.,Barford, D.,Nakamura, Y.,Song, H.
Crystal structure and functional analysis of the eukaryotic class II release factor eRF3 from S. pombe
Mol.Cell, 14:233-245, 2004

PubMed Abstract: Translation termination in eukaryotes is governed by two interacting release factors, eRF1 and eRF3. The crystal structure of the eEF1alpha-like region of eRF3 from S. pombe determined in three states (free protein, GDP-, and GTP-bound forms) reveals an overall structure that is similar to EF-Tu, although with quite different domain arrangements. In contrast to EF-Tu, GDP/GTP binding to eRF3c does not induce dramatic conformational changes, and Mg(2+) is not required for GDP binding to eRF3c. Mg(2+) at higher concentration accelerates GDP release, suggesting a novel mechanism for nucleotide exchange on eRF3 from that of other GTPases. Mapping sequence conservation onto the molecular surface, combined with mutagenesis analysis, identified the eRF1 binding region, and revealed an essential function for the C terminus of eRF3. The N-terminal extension, rich in acidic amino acids, blocks the proposed eRF1 binding site, potentially regulating eRF1 binding to eRF3 in a competitive manner.

PubMed: 15099522
DOI: 10.1016/S1097-2765(04)00206-0

Experimental method

X-RAY DIFFRACTION (3.2 Å)