2bht

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(New page: 200px<br /><applet load="2bht" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bht, resolution 2.10&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:2bht.gif|left|200px]]<br /><applet load="2bht" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2bht, resolution 2.10&Aring;" />
caption="2bht, resolution 2.10&Aring;" />
'''CRYSTAL STRUCTURE OF O-ACETYLSERINE SULFHYDRYLASE B'''<br />
'''CRYSTAL STRUCTURE OF O-ACETYLSERINE SULFHYDRYLASE B'''<br />
==Overview==
==Overview==
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The enzyme O-acetylserine sulfhydrylase participates in the biosynthesis, of l-cysteine in bacteria and plants. The structure of isoenzyme B (CysM), from Escherichia coli was established in a hexagonal crystal form at 2.7 A, resolution (wild-type) and in a merohedrally twinned tetragonal crystal, form at 2.1 A resolution (surface mutant). Structural superpositions, revealed the variations with respect to isoenzyme A (CysK) and explained, the different substrate specificities. A geometric model of the reaction, catalyzed by CysM is proposed. Both isoenzymes are used for the production, of l-amino acid derivatives as building blocks for the synthesis of, peptides and peptidomimetic drugs. Since the structure of CysM revealed a, remarkable main chain variation at the active center, it constitutes a, further starting point for engineering mutants with novel substrate, specificities.
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The enzyme O-acetylserine sulfhydrylase participates in the biosynthesis of l-cysteine in bacteria and plants. The structure of isoenzyme B (CysM) from Escherichia coli was established in a hexagonal crystal form at 2.7 A resolution (wild-type) and in a merohedrally twinned tetragonal crystal form at 2.1 A resolution (surface mutant). Structural superpositions revealed the variations with respect to isoenzyme A (CysK) and explained the different substrate specificities. A geometric model of the reaction catalyzed by CysM is proposed. Both isoenzymes are used for the production of l-amino acid derivatives as building blocks for the synthesis of peptides and peptidomimetic drugs. Since the structure of CysM revealed a remarkable main chain variation at the active center, it constitutes a further starting point for engineering mutants with novel substrate specificities.
==About this Structure==
==About this Structure==
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2BHT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/Cysteine_synthase Cysteine synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.47 2.5.1.47] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BHT OCA].
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2BHT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/Cysteine_synthase Cysteine synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.47 2.5.1.47] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BHT OCA].
==Reference==
==Reference==
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Claus, M.T.]]
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[[Category: Claus, M T.]]
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[[Category: Maier, T.H.P.]]
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[[Category: Maier, T H.P.]]
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[[Category: Schulz, G.E.]]
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[[Category: Schulz, G E.]]
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[[Category: Zocher, G.E.]]
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[[Category: Zocher, G E.]]
[[Category: cysteine biosynthesis]]
[[Category: cysteine biosynthesis]]
[[Category: plp-dependent enzyme]]
[[Category: plp-dependent enzyme]]
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[[Category: transferase]]
[[Category: transferase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:47:43 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:37:57 2008''

Revision as of 14:38, 21 February 2008


2bht, resolution 2.10Å

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CRYSTAL STRUCTURE OF O-ACETYLSERINE SULFHYDRYLASE B

Overview

The enzyme O-acetylserine sulfhydrylase participates in the biosynthesis of l-cysteine in bacteria and plants. The structure of isoenzyme B (CysM) from Escherichia coli was established in a hexagonal crystal form at 2.7 A resolution (wild-type) and in a merohedrally twinned tetragonal crystal form at 2.1 A resolution (surface mutant). Structural superpositions revealed the variations with respect to isoenzyme A (CysK) and explained the different substrate specificities. A geometric model of the reaction catalyzed by CysM is proposed. Both isoenzymes are used for the production of l-amino acid derivatives as building blocks for the synthesis of peptides and peptidomimetic drugs. Since the structure of CysM revealed a remarkable main chain variation at the active center, it constitutes a further starting point for engineering mutants with novel substrate specificities.

About this Structure

2BHT is a Single protein structure of sequence from Escherichia coli. Active as Cysteine synthase, with EC number 2.5.1.47 Full crystallographic information is available from OCA.

Reference

Structure of the O-acetylserine sulfhydrylase isoenzyme CysM from Escherichia coli., Claus MT, Zocher GE, Maier TH, Schulz GE, Biochemistry. 2005 Jun 21;44(24):8620-6. PMID:15952768

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