Structure of L-arabinose-binding protein from Escherichia coli at 5 A resolution and preliminary results at 3.5 A.
- 1 July 1976
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 73 (7) , 2186-2190
- https://doi.org/10.1073/pnas.73.7.2186
Abstract
The 3-dimensional crystal structure of the L-arabinose-binding protein from E. coli, an essential component in the active transport of L-arabinose, was resolved at 5 .ANG. resolution using the method of multiple isomorphous replacement. Five heavy atom derivatives were used. A preliminary 3.5 .ANG. electron density map was also calculated. The molecule is ellipsoidal with approximate dimensions 68 .ANG. .times. 38 .ANG. .times. 30 .ANG.. Two similar domains within the molecule (which is a single polypeptide chain) are related by an approximate noncrystallographic rotation-translation axis. This relationship involves approximately 20% of the structure.Keywords
This publication has 10 references indexed in Scilit:
- Preliminary crystallographic data for a calcium binding protein from bovine intestineJournal of Molecular Biology, 1975
- Chemotaxis in BacteriaAnnual Review of Biochemistry, 1975
- A Comparison of the l-Arabinose- and d-Galactose-binding Proteins of Escherichia coli B/rJournal of Biological Chemistry, 1974
- Crystallographic data of an l-arabinose-binding protein from Escherichia coliJournal of Molecular Biology, 1974
- Crystallization and Characterization of the l-Arabinose-binding Protein of Escherichia coli B/rJournal of Biological Chemistry, 1974
- Bacterial TransportAnnual Review of Biochemistry, 1974
- Membrane Transport ProteinsPublished by Springer Nature ,1974
- Design of a diffractometer and flow cell system for X-ray analysis of crystalline proteins with applications to the crystal chemistry of ribonuclease-SJournal of Molecular Biology, 1967
- The structure of carboxypeptidase AJournal of Molecular Biology, 1966