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'''CRYSTAL STRUCTURE OF O-ACETYLSERINE SULFHYDRYLASE B''' | '''CRYSTAL STRUCTURE OF O-ACETYLSERINE SULFHYDRYLASE B''' | ||
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[[Category: Schulz, G E.]] | [[Category: Schulz, G E.]] | ||
[[Category: Zocher, G E.]] | [[Category: Zocher, G E.]] | ||
[[Category: | [[Category: Cysteine biosynthesis]] | ||
[[Category: | [[Category: Plp-dependent enzyme]] | ||
[[Category: | [[Category: Pyridoxal phosphate]] | ||
[[Category: | [[Category: Pyridoxal-5'-phosphate]] | ||
[[Category: | [[Category: Transferase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 20:18:32 2008'' | |||
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Revision as of 17:18, 3 May 2008
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. 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 Page seeded by OCA on Sat May 3 20:18:32 2008
