Structure of the C-terminal domain of the ribosomal protein L7/L12 from Escherichia coli at 1.7 A

M Leijonmarck; A Liljas

doi:10.1016/0022-2836(87)90183-5

Structure of the C-terminal domain of the ribosomal protein L7/L12 from Escherichia coli at 1.7 A

J Mol Biol. 1987 Jun 5;195(3):555-79. doi: 10.1016/0022-2836(87)90183-5.

Authors

M Leijonmarck¹, A Liljas

Affiliation

¹ Institute of Molecular Biology, University of Uppsala, Sweden.

PMID: 3309338
DOI: 10.1016/0022-2836(87)90183-5

Abstract

The structure of a C-terminal fragment of the ribosomal protein L7/L12 from Escherichia coli has been refined using crystallographic data to 1.7 A resolution. The R-value is 17.4%. Six residues at the N terminus are too disordered in the structure to be localized. These residues are probably part of a hinge in the complete L7/L12 molecule. The possibility that a 2-fold crystallographic axis is a molecular 2-fold axis is discussed. A patch of invariant residues on the surface of the dimer is probably involved in functional interactions with elongation factors.

Publication types

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

MeSH terms

Amino Acid Sequence
Bacterial Proteins*
Crystallography
Escherichia coli / analysis
Hydrogen Bonding
Models, Molecular
Protein Conformation
Ribosomal Proteins*

Substances

Bacterial Proteins
Ribosomal Proteins
ribosomal protein L7-L12