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Protein Engineering vol. 1 no. 6 pp. 467-469, 1987
© 1987 Oxford University Press

OTHER

Comparison of backbone structures of glucose isomerase from Streptomyces and Arthrobacter

K. Henrick, D.M. Blow, H.L. Carrell and J.P. Glusker

Blackett Laboratory, Imperial College London, SW7 2BZ, UK Institute for Cancer Research, Fox Chase Cancer Center 7701 Burholme Avenue, Philadelphia, PA 19111, USA

The C{alpha} backbones of the glucose isomerase molecules of Streptomyces rubiginosus and Arthrobacter have been determined by X-ray crystallography and compared. Each molecule is a tetramer of eight-stranded {alpha}/ß barrels, and the mode of association of the tetramers is identical in each case. The Arthrobacter electron density shows four additional amino acids at the carboxyl terminus. There is also an insertion of six amino acids at position 277, and two individual insertions at about positions 348 and 357 (numbering according to the Streptomyces structure). There is a close structural homology throughout the whole molecule, which is most accurate up to position 325. The r.m.s. displacement for 315 homologous C{alpha} positions up to this position is 0.92 Å.

Keywords: glucose isomerase/backbone structure/X-ray crystallography

Received September 28, 1987; revised November 17, 1987;
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