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Literature summary for 2.7.3.2 extracted from

  • Ohren, J.F.; Kundracik, M.L.; Borders, C.L.; Edmiston, P.; Viola, R.E.
    Structural asymmetry and intersubunit communication in muscle creatine kinase (2007), Acta Crystallogr. Sect. D, 63, 381-389.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
structure of mutant R134K in a transition-state analogue complex. The functional enzyme dimer shows significant structural asymmetry with one monomer in a closed conformation with the active site occupied by the transition-state analogue components craetine, MgADP and nitrate. The other monomer has the two loops that control access to the active site in an open conformation and only MgADP is bound Oryctolagus cuniculus

Protein Variants

Protein Variants Comment Organism
additional information deletion of N-terminal 15 amino acids causes dissociation of the functional homodimer into monomers with reduced catalytic activity Oryctolagus cuniculus
P20G disruption of subunit cohesion, causing dissociation of the functional homodimer into monomers with reduced catalytic activity Oryctolagus cuniculus
R134K highly soluble mutant, crystallization data Oryctolagus cuniculus

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus P00563
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Source Tissue

Source Tissue Comment Organism Textmining
muscle
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Oryctolagus cuniculus
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