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Literature summary for 1.4.4.2 extracted from

  • Nakai, T.; Nakagawa, N.; Maoka, N.; Masui, R.; Kuramitsu, S.; Kamiya, N.
    Structure of P-protein of the glycine cleavage system: implications for nonketotic hyperglycinemia (2005), EMBO J., 24, 1523-1536.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
vapour diffusion method with 30% w/v polyethylene glycol 3350 and 100 mM KSCN as the precipitant. Crystal structure of three forms of P-protein: the apoenzyme at 2.4 A resolution, the holoenzyme at 2.1 A resolution and the holoenzyme in complex with a substrate analog inhibitor (aminooxy)acetate Thermus thermophilus

Inhibitors

Inhibitors Comment Organism Structure
Aminooxyacetate
-
Thermus thermophilus

Organism

Organism UniProt Comment Textmining
Thermus thermophilus
-
-
-
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
-
-

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate binding to the apoenzyme induces large open-closed conformational changes, with residues moving up to 13.5 A Thermus thermophilus