Open AccessStructure of L-arabinose-binding protein from Escherichia coli at 5 A resolution and preliminary results at 3.5 A.
Author(s) -
G.N. Phillips,
Vikram K. Mahajan,
A K Siu,
Florante A. Quiocho
Publication year - 1976
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.73.7.2186
Subject(s) - translation (biology) , resolution (logic) , arabinose , molecule , crystallography , escherichia coli , multiple isomorphous replacement , chemistry , rotation (mathematics) , atom (system on chip) , polypeptide chain , crystal structure , geometry , peptide sequence , biochemistry , mathematics , amino acid , gene , computer science , artificial intelligence , fermentation , messenger rna , organic chemistry , embedded system , xylose
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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