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. 1976 Jul;73(7):2186-90.
doi: 10.1073/pnas.73.7.2186.

Structure of L-arabinose-binding protein from Escherichia coli at 5 A resolution and preliminary results at 3.5 A

G N Phillips Jr, V K Mahajan, A K Siu, F A Quiocho

Structure of L-arabinose-binding protein from Escherichia coli at 5 A resolution and preliminary results at 3.5 A

G N Phillips Jr et al. Proc Natl Acad Sci U S A. 1976 Jul.

Abstract

The three-dimensional crystal structure of the L-arabinose-binding protein from E. coli, an essential component in the active transport of L-arabinose, has been solved at 5 A resolution using the method of multiple isomorphous replacement. Five heavy atom derivatives were used. A preliminary 3.5 A electron density map has also been calculated. The results indicate that the molecule is ellipsoidal with approximate dimensions 68 A X 38 A X 30 A. 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.

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