1GQE

Polypeptide Chain Release Factor 2 (RF2) from Escherichia coli

Summary for 1GQE

• Entry DOI: 10.2210/pdb1gqe/pdb
• Descriptor: RELEASE FACTOR 2 (2 entities in total)
• Functional Keywords: protein synthesis, ribosome, macromolecular mimicry, translation
• Biological source: ESCHERICHIA COLI
• Total number of polymer chains: 1
• Total formula weight: 41678.66

Authors

Vestergaard, B.,Kjeldgaard, M. (deposition date: 2001-11-22, release date: 2002-04-04, Last modification date: 2024-10-16)

Primary citation

Vestergaard, B.,Van, L.,Andersen, G.,Nyborg, J.,Buckingham, R.,Kjeldgaard, M.
Bacterial Polypeptide Release Factor Rf2 is Structurally Distinct from Eukaryotic Erf1.
Mol.Cell, 8:1375-, 2001

PubMed Abstract: Bacterial release factor RF2 promotes termination of protein synthesis, specifically recognizing stop codons UAA or UGA. The crystal structure of Escherichia coli RF2 has been determined to a resolution of 1.8 A. RF2 is structurally distinct from its eukaryotic counterpart eRF1. The tripeptide SPF motif, thought to confer RF2 stop codon specificity, and the universally conserved GGQ motif, proposed to be involved with the peptidyl transferase center, are exposed in loops only 23 A apart, and the structure suggests that stop signal recognition is more complex than generally believed.

PubMed: 11779511
DOI: 10.1016/S1097-2765(01)00415-4

Experimental method

X-RAY DIFFRACTION (1.81 Å)