Crystallization (Comment) | Organism |
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analysis of high-resolution vibrational spectral fingerprints of each substrate and intermediate. The bound IMP is distorted toward its N1-deprotonated form even in the absence of any other ligands. Specific interactions between GTP and active-site amino acid residues result in large Raman shifts and contribute substantially to intrinsic binding energy. When both IMP and GTP are simultaneously bound, IMP is converted into an intermediate 6-phosphoryl inosine 5'-monophosphate. The intermediate complex is stable upon binding of the third ligand, L-aspartae analogue hadaicin. In the absence of hadaicin, 6-phosphoryl inosine 5'-monophosphate is quickly released from ADSS, is unstable in solution, and converts back into IMP. Hadaicin allosterically stabilizes ADSS through local conformational rearrangements | Methanocaldococcus jannaschii |
Organism | UniProt | Comment | Textmining |
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Methanocaldococcus jannaschii | Q57981 | - |
- |
Methanocaldococcus jannaschii DSM 2661 | Q57981 | - |
- |
Synonyms | Comment | Organism |
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purA | - |
Methanocaldococcus jannaschii |