1csm

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(New page: 200px<br /><applet load="1csm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1csm, resolution 2.2&Aring;" /> '''THE CRYSTAL STRUCTURE...)
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[[Image:1csm.gif|left|200px]]<br /><applet load="1csm" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1csm, resolution 2.2&Aring;" />
caption="1csm, resolution 2.2&Aring;" />
'''THE CRYSTAL STRUCTURE OF ALLOSTERIC CHORISMATE MUTASE AT 2.2 ANGSTROMS RESOLUTION'''<br />
'''THE CRYSTAL STRUCTURE OF ALLOSTERIC CHORISMATE MUTASE AT 2.2 ANGSTROMS RESOLUTION'''<br />
==Overview==
==Overview==
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The crystal structure of an allosteric chorismate mutase, the, Thr-226--&gt;Ile mutant, from yeast Saccharomyces cerevisiae has been, determined to 2.2-A resolution by using the multiple isomorphous, replacement method. Solvent-flattening and electron-density modification, were applied for phase improvement. The current crystallographic R factor, is 0.196. The final model includes 504 of the 512 residues and 97 water, molecules. In addition, two tryptophan molecules were identified in the, interface between monomers. The overall structure is completely different, from the reported structure of chorismate mutase from Bacillus subtilis., This structure showed 71% helices with essentially no beta-sheet, structures.
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The crystal structure of an allosteric chorismate mutase, the Thr-226--&gt;Ile mutant, from yeast Saccharomyces cerevisiae has been determined to 2.2-A resolution by using the multiple isomorphous replacement method. Solvent-flattening and electron-density modification were applied for phase improvement. The current crystallographic R factor is 0.196. The final model includes 504 of the 512 residues and 97 water molecules. In addition, two tryptophan molecules were identified in the interface between monomers. The overall structure is completely different from the reported structure of chorismate mutase from Bacillus subtilis. This structure showed 71% helices with essentially no beta-sheet structures.
==About this Structure==
==About this Structure==
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1CSM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with TRP as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Anthranilate_synthase Anthranilate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.3.27 4.1.3.27] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CSM OCA].
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1CSM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=TRP:'>TRP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Anthranilate_synthase Anthranilate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.3.27 4.1.3.27] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CSM OCA].
==Reference==
==Reference==
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Lipscomb, W.N.]]
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[[Category: Lipscomb, W N.]]
[[Category: Xue, Y.]]
[[Category: Xue, Y.]]
[[Category: TRP]]
[[Category: TRP]]
[[Category: isomerase]]
[[Category: isomerase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:43:34 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:09:18 2008''

Revision as of 10:09, 21 February 2008


1csm, resolution 2.2Å

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THE CRYSTAL STRUCTURE OF ALLOSTERIC CHORISMATE MUTASE AT 2.2 ANGSTROMS RESOLUTION

Overview

The crystal structure of an allosteric chorismate mutase, the Thr-226-->Ile mutant, from yeast Saccharomyces cerevisiae has been determined to 2.2-A resolution by using the multiple isomorphous replacement method. Solvent-flattening and electron-density modification were applied for phase improvement. The current crystallographic R factor is 0.196. The final model includes 504 of the 512 residues and 97 water molecules. In addition, two tryptophan molecules were identified in the interface between monomers. The overall structure is completely different from the reported structure of chorismate mutase from Bacillus subtilis. This structure showed 71% helices with essentially no beta-sheet structures.

About this Structure

1CSM is a Single protein structure of sequence from Saccharomyces cerevisiae with as ligand. Active as Anthranilate synthase, with EC number 4.1.3.27 Full crystallographic information is available from OCA.

Reference

The crystal structure of allosteric chorismate mutase at 2.2-A resolution., Xue Y, Lipscomb WN, Graf R, Schnappauf G, Braus G, Proc Natl Acad Sci U S A. 1994 Nov 8;91(23):10814-8. PMID:7971967

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