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Literature summary for 2.5.1.65 extracted from

  • Jurgenson, C.T.; Burns, K.E.; Begley, T.P.; Ealick, S.E.
    Crystal structure of a sulfur carrier protein complex found in the cysteine biosynthetic pathway of Mycobacterium tuberculosis (2008), Biochemistry, 47, 10354-10364.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli as a His-tagged fusion protein Mycobacterium tuberculosis

Crystallization (Commentary)

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

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

Organism UniProt Comment Textmining
Mycobacterium tuberculosis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
using Ni-NTA chromatography Mycobacterium tuberculosis

Subunits

Subunits Comment Organism
dimer crystal structure Mycobacterium tuberculosis

Synonyms

Synonyms Comment Organism
CysM
-
Mycobacterium tuberculosis
Rv1336
-
Mycobacterium tuberculosis

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate
-
Mycobacterium tuberculosis