1xia
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(New page: 200px<br /><applet load="1xia" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xia, resolution 2.3Å" /> '''COMPARISON OF BACKBON...)
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Revision as of 00:05, 25 November 2007
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COMPARISON OF BACKBONE STRUCTURES OF GLUCOSE ISOMERASE FROM STREPTOMYCES AND ARTHROBACTER
Overview
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.
About this Structure
1XIA is a Protein complex structure of sequences from [1]. Active as Xylose isomerase, with EC number 5.3.1.5 Full crystallographic information is available from OCA.
Reference
Comparison of backbone structures of glucose isomerase from Streptomyces and Arthrobacter., Henrick K, Blow DM, Carrell HL, Glusker JP, Protein Eng. 1987 Dec;1(6):467-9. PMID:3508294
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