Cloned (Comment) | Organism |
---|---|
expressed in Escherichia coli as a His-tagged fusion protein | Mycobacterium tuberculosis |
Crystallization (Comment) | Organism |
---|---|
the structure of the protein complex CysM-CysO is determined at 1.53 A resolution. The protein complex in the crystal structure is asymmetric with one CysO (sulfur carrier protein) protomer binding to one end of a CysM dimer. The structures of CysM is determined individually at 2.8 A resolution. Sequence alignments with homologues and structural comparisons with CysK, a cysteine synthase that does not utilize a sulfur carrier protein, reveal high conservation of active site residues, but residues in CysM responsible for CysO binding are not conserved | Mycobacterium tuberculosis |
Protein Variants | Comment | Organism |
---|---|---|
K204A | to improve crystallization of CysM alone, a putative surface residue in CysM (Lys204) is mutated to alanine using site-directed mutagenesis | Mycobacterium tuberculosis |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mycobacterium tuberculosis | - |
- |
- |
Purification (Comment) | Organism |
---|---|
using Ni-NTA chromatography | Mycobacterium tuberculosis |
Subunits | Comment | Organism |
---|---|---|
dimer | crystal structure | Mycobacterium tuberculosis |
Synonyms | Comment | Organism |
---|---|---|
CysM | - |
Mycobacterium tuberculosis |
Rv1336 | - |
Mycobacterium tuberculosis |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
pyridoxal 5'-phosphate | - |
Mycobacterium tuberculosis |