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Literature summary for 2.7.7.62 extracted from

  • Singarapu, K.K.; Otte, M.M.; Tonelli, M.; Westler, W.M.; Escalante-Semerena, J.C.; Markley, J.L.
    Solution structural studies of GTP:adenosylcobinamide-phosphateguanylyl transferase (CobY) from Methanocaldococcus jannaschii (2015), PLoS ONE, 10, e0141297.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Protein Variants Comment Organism
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

Organism UniProt Comment Textmining
Methanocaldococcus jannaschii Q58517
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Methanocaldococcus jannaschii DSM 2661 Q58517
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Subunits

Subunits Comment Organism
monomer wild-type CobY is monomeric in solution in both its apo- and GTP-bound formssolution structural studies Methanocaldococcus jannaschii

Synonyms

Synonyms Comment Organism
CobY
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Methanocaldococcus jannaschii