Crystallization (Comment) | Organism |
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the solution structure has a mixed alpha/beta fold consisting of seven beta-strands and five alpha-helices, very similar to a Rossmann fold. Titration of apo-CobY with GTP results in large changes in amide proton chemical shifts. The CobY:GTP complex is unstable over time, GTP hydrolyzes and the protein converts slowly to a species with an NMR spectrum similar to that of apo-CobY. The variant CobYG153D, yields NMR spectra similar to those of wild-type CobY in both its apo-state and in complex with GTP. The CobYG153D:GTP complex is also unstable over time | Methanocaldococcus jannaschii |
Protein Variants | Comment | Organism |
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G153D | residues R13 and K19 of the mutant directly coordinate the phosphate group of GTP in the X-ray structure. The X-ray structure of the CobYG153D:GTP complex is modeled as a homodimer | Methanocaldococcus jannaschii |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Methanocaldococcus jannaschii | Q58517 | - |
- |
Methanocaldococcus jannaschii DSM 2661 | Q58517 | - |
- |
Subunits | Comment | Organism |
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monomer | wild-type CobY is monomeric in solution in both its apo- and GTP-bound formssolution structural studies | Methanocaldococcus jannaschii |
Synonyms | Comment | Organism |
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CobY | - |
Methanocaldococcus jannaschii |