The three‐dimensional structure of the colicin E3 immunity protein by distance geometry calculation
Open Access
- 12 November 1993
- journal article
- Published by Wiley in FEBS Letters
- Vol. 333 (3), 257-260
- https://doi.org/10.1016/0014-5793(93)80665-h
Abstract
The three‐dimensional solution structure of the colicin E3 immunity protein (84 residues) was determined by distance geometry calculations. The hydrophilic side of a four‐stranded antiparallel β‐sheet constitutes a part of the surface of the protein, and two loops lie on the hydrophobic side of the sheet. All the three specificity‐determining residues, which are included in the center of the β‐sheet, display their side groups on the protein surface.Keywords
This publication has 19 references indexed in Scilit:
- The structure of ribosomal protein S5 reveals sites of interaction with 16S rRNANature, 1992
- Proton, carbon-13, and nitrogen-15 NMR assignments and global folding pattern of the RNA-binding domain of the human hnRNP C proteinsBiochemistry, 1992
- Presto(protein engineering simulator): A vectorized molecular mechanics program for biopolymersComputers & Chemistry, 1992
- The secondary structure of the colicin E3 immunity protein as studied by proton-proton and proton-nitrogen-15 two-dimensional NMR spectroscopyBiochemistry, 1992
- Identification of a unique specificity determinant of the colicin E3 immunity proteinGene, 1991
- Crystal structure of the RNA-binding domain of the U1 small nuclear ribonucleoprotein ANature, 1990
- An all atom force field for simulations of proteins and nucleic acidsJournal of Computational Chemistry, 1986
- Colicin E3 and its immunity genesJournal of Molecular Biology, 1985
- Assignment of the functional loci in colicin E2 and E3 molecules by the characterization of their proteolytic fragmentsBiochemistry, 1980
- Inactivation of bacterial ribosome in vivo and in vitro by cloacin DF13FEBS Letters, 1973