2bht
From Proteopedia
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| , resolution 2.10Å | |||||||
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| Activity: | Cysteine synthase, with EC number 2.5.1.47 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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