Structural determination of the functional sites of E. coli elongation factor Tu

B F Clark; M Kjeldgaard; T F la Cour; S Thirup; J Nyborg

doi:10.1016/0167-4781(90)90167-z

Structural determination of the functional sites of E. coli elongation factor Tu

Biochim Biophys Acta. 1990 Aug 27;1050(1-3):203-8. doi: 10.1016/0167-4781(90)90167-z.

Authors

B F Clark¹, M Kjeldgaard, T F la Cour, S Thirup, J Nyborg

Affiliation

¹ Department of Chemistry, Aarhus University, Denmark.

PMID: 2207145
DOI: 10.1016/0167-4781(90)90167-z

Abstract

Recently, we have made significant progress in solving the structure of a nicked form of elongation factor (EF)-Tu complexed with GDP. The structure has been refined to an R factor of 19.2% at 2.6 A resolution, so that most of the structure is clearly visible in the electron density map. Here we describe what is known about functional sites of EF-Tu in terms of the structure, which still lacks amino acids 40-60.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Anti-Bacterial Agents / metabolism
Binding Sites
Escherichia coli / metabolism*
Guanosine Diphosphate / metabolism
Models, Molecular
Peptide Elongation Factor Tu / chemistry
Peptide Elongation Factor Tu / metabolism*
Protein Conformation
Pyridones / metabolism
RNA, Transfer, Amino Acyl / metabolism
X-Ray Diffraction

Substances

Anti-Bacterial Agents
Pyridones
RNA, Transfer, Amino Acyl
Guanosine Diphosphate
Peptide Elongation Factor Tu
mocimycin