1odt

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(New page: 200px<br /> <applet load="1odt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1odt, resolution 1.70&Aring;" /> '''CEPHALOSPORIN C DEA...)
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==About this Structure==
==About this Structure==
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1ODT is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]] with ACT as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.41 3.1.1.41]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ODT OCA]].
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1ODT is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]] with ACT as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/Cephalosporin-C_deacetylase Cephalosporin-C deacetylase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.41 3.1.1.41]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ODT OCA]].
==Reference==
==Reference==
Multifunctional xylooligosaccharide/cephalosporin C deacetylase revealed by the hexameric structure of the Bacillus subtilis enzyme at 1.9A resolution., Vincent F, Charnock SJ, Verschueren KH, Turkenburg JP, Scott DJ, Offen WA, Roberts S, Pell G, Gilbert HJ, Davies GJ, Brannigan JA, J Mol Biol. 2003 Jul 11;330(3):593-606. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12842474 12842474]
Multifunctional xylooligosaccharide/cephalosporin C deacetylase revealed by the hexameric structure of the Bacillus subtilis enzyme at 1.9A resolution., Vincent F, Charnock SJ, Verschueren KH, Turkenburg JP, Scott DJ, Offen WA, Roberts S, Pell G, Gilbert HJ, Davies GJ, Brannigan JA, J Mol Biol. 2003 Jul 11;330(3):593-606. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12842474 12842474]
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
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[[Category: Cephalosporin-C deacetylase]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Brannigan, J.A.]]
[[Category: Brannigan, J.A.]]
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[[Category: x-ray structure]]
[[Category: x-ray structure]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 20:49:52 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 13:35:56 2007''

Revision as of 11:31, 30 October 2007


1odt, resolution 1.70Å

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CEPHALOSPORIN C DEACETYLASE MUTATED, IN COMPLEX WITH ACETATE

Overview

Esterases and deacetylases active on carbohydrate ligands have been, classified into 14 families based upon amino acid sequence similarities., Enzymes from carbohydrate esterase family seven (CE-7) are unusual in that, they display activity towards both acetylated xylooligosaccharides and the, antibiotic, cephalosporin C. The 1.9A structure of the multifunctional, CE-7 esterase (hereinafter CAH) from Bacillus subtilis 168 reveals a, classical alpha/beta hydrolase fold encased within a 32 hexamer. This is, the first example of a hexameric alpha/beta hydrolase and is further, evidence of the versatility of this particular fold, which is used in a, wide variety of biological contexts. A narrow entrance tunnel leads to the, centre of the molecule, where the six active-centre catalytic triads ... [(full description)]

About this Structure

1ODT is a [Single protein] structure of sequence from [Bacillus subtilis] with ACT as [ligand]. Active as [Cephalosporin-C deacetylase], with EC number [3.1.1.41]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Multifunctional xylooligosaccharide/cephalosporin C deacetylase revealed by the hexameric structure of the Bacillus subtilis enzyme at 1.9A resolution., Vincent F, Charnock SJ, Verschueren KH, Turkenburg JP, Scott DJ, Offen WA, Roberts S, Pell G, Gilbert HJ, Davies GJ, Brannigan JA, J Mol Biol. 2003 Jul 11;330(3):593-606. PMID:12842474

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