2bht

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{{STRUCTURE_2bht| PDB=2bht | SCENE= }}
{{STRUCTURE_2bht| PDB=2bht | SCENE= }}
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'''CRYSTAL STRUCTURE OF O-ACETYLSERINE SULFHYDRYLASE B'''
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===CRYSTAL STRUCTURE OF O-ACETYLSERINE SULFHYDRYLASE B===
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==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 line below this paragraph, {{ABSTRACT_PUBMED_15952768}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 15952768 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15952768}}
==About this Structure==
==About this Structure==
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[[Category: Pyridoxal-5'-phosphate]]
[[Category: Pyridoxal-5'-phosphate]]
[[Category: Transferase]]
[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 20:18:32 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 12:15:15 2008''

Revision as of 09:15, 29 July 2008

Image:2bht.png

Template:STRUCTURE 2bht

CRYSTAL STRUCTURE OF O-ACETYLSERINE SULFHYDRYLASE B

Template:ABSTRACT PUBMED 15952768

About this Structure

2BHT is a Single protein structure of sequence from Escherichia coli. 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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