2BHS
Crystal Structure of Cysteine Synthase B
Summary for 2BHS
| Entry DOI | 10.2210/pdb2bhs/pdb |
| Related | 2BHT |
| Descriptor | CYSTEINE SYNTHASE B, PYRIDOXAL-5'-PHOSPHATE (3 entities in total) |
| Functional Keywords | cysteine biosynthesis, plp-dependent enzyme, pyridoxal-5'-phosphate, pyridoxal phosphate, transferase |
| Biological source | ESCHERICHIA COLI |
| Total number of polymer chains | 4 |
| Total formula weight | 131784.98 |
| Authors | Claus, M.T.,Zocher, G.E.,Maier, T.H.P.,Schulz, G.E. (deposition date: 2005-01-18, release date: 2005-06-22, Last modification date: 2011-07-13) |
| Primary citation | Claus, M.T.,Zocher, G.E.,Maier, T.H.P.,Schulz, G.E. Structure of the O-Acetylserine Sulfhydrylase Isoenzyme Cysm from Escherichia Coli Biochemistry, 44:8620-, 2005 Cited by PubMed Abstract: 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. PubMed: 15952768DOI: 10.1021/BI050485+ PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.67 Å) |
Structure validation
Download full validation report
