Refined structure of elongation factor EF-Tu from Escherichia coli.

doi:10.1016/0022-2836(92)90986-t

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Article

Refined structure of elongation factor EF-Tu from Escherichia coli.

Journal of molecular biology - 5 Feb 1992

Kjeldgaard M, Nyborg J

Abstract excerpt

The crystal structure of trypsin-modified elongation factor Tu from Escherichia coli, in complex with the cofactor guanosine diphosphate has been refined to a crystallographic R-factor of 19.3%, at 2.6 A resolution. In the model described, the root-mean-square deviation from ideality is 0.019 A f...

Topics

Amino Acid Sequence
Binding Sites
Escherichia coli
GTP-Binding Proteins
Guanine
Guanosine Diphosphate
Hydrogen Bonding
Magnesium
Models, Molecular
Molecular Sequence Data
Mutation
Peptide Elongation Factor Tu
Phosphates
Protein Conformation
Proto-Oncogene Proteins p21(ras)
Ribose
Sequence Alignment
X-Ray Diffraction

Source

Open in PubMed

Identifiers

PMID: 1542116
DOI: 10.1016/0022-2836(92)90986-t

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-1542116-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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