Comparison of backbone structures of glucose isomerase from Streptomyces and Arthrobacter.
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Henrick K, Blow DM, Carrell HL, Glusker JP
Comparison of backbone structures of glucose isomerase from Streptomyces and Arthrobacter.
Protein Eng. 1987 Dec;1(6):467-9.
- PubMed ID
- 3508294 [ View in PubMed]
- Abstract
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/beta 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 A.