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Title
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Comparison of backbone structures of glucose isomerase from Streptomyces and Arthrobacter.
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Authors
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K.Henrick,
D.M.Blow,
H.L.Carrell,
J.P.Glusker.
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Ref.
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Protein Eng, 1987,
1,
467-469.
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PubMed id
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Abstract
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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.
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