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 2.10Å" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 06:40, 21 November 2007
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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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