Literature summary extracted from
Martinez-Cruz, L.A.; Dreyer, M.K.; Boisvert, D.C.; Yokota, H.; Martinez-Chantar, M.L.; Kim, R.; Kim, S.
Crystal structure of MJ1247 protein from M. jannaschii at 2.0 A resolution infers a molecular function of 3-hexulose-6-phosphate isomerase (2002), Structure, 10, 195-204.
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
5.3.1.27 |
expression in Escherichia coli |
Methanocaldococcus jannaschii |
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
5.3.1.27 |
diffraction to 2.0 A resolution. MJ1247 is an alpha/beta structure consisting of a five-stranded parallel beta-sheet flanked on both sides by alpha-helices, forming a three-layered alpha-beta-alpha sandwich. The fold represents the nucleotide binding motif of a flavodoxin type. Protein forms a tetramer in the crystal an in solution and each monomer has a folding similar to the isomerase domain of glucosamine 6-phosphate synthase |
Methanocaldococcus jannaschii |
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
5.3.1.27 |
Methanocaldococcus jannaschii |
Q58644 |
- |
- |