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 2.3&Aring;" /> '''COMPARISON OF BACKBON...)
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'''COMPARISON OF BACKBONE STRUCTURES OF GLUCOSE ISOMERASE FROM STREPTOMYCES AND ARTHROBACTER'''<br />
'''COMPARISON OF BACKBONE STRUCTURES OF GLUCOSE ISOMERASE FROM STREPTOMYCES AND ARTHROBACTER'''<br />
==Overview==
==Overview==
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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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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==
==About this Structure==
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1XIA is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Active as [http://en.wikipedia.org/wiki/Xylose_isomerase Xylose isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.5 5.3.1.5] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1XIA OCA].
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1XIA is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Active as [http://en.wikipedia.org/wiki/Xylose_isomerase Xylose isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.5 5.3.1.5] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XIA OCA].
==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Xylose isomerase]]
[[Category: Xylose isomerase]]
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[[Category: Blow, D.M.]]
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[[Category: Blow, D M.]]
[[Category: isomerase(intramolecular oxidoreductse)]]
[[Category: isomerase(intramolecular oxidoreductse)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 02:13:01 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:55:06 2008''

Revision as of 13:55, 21 February 2008


1xia, resolution 2.3Å

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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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