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Literature summary for 1.5.1.3 extracted from

  • Chen, J.; Dima, R.I.; Thirumalai, D.
    Allosteric communication in dihydrofolate reductase: signaling network and pathways for closed to occluded transition and back (2007), J. Mol. Biol., 374, 250-266.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
self-organized polymer model to monitor the kinetics of closed to occluded and reverse transitions. During the closed to occluded transition, coordinated changes in a number of residues in the loop domain enable the M20 loop to slide along the alpha-helix in the adenosine-binding domain. Sliding is triggered by pulling of the M20 loop by the betaG-betaH loop and the pushing action of the betaG-betaH loop. The residues that facilitate the M20 loop motion are part of the network of residues that transmit allosteric signals during the close to occluded transition. Replacement of M16 and G121 by a disulfide cross-link impedes that transition. The order of events in the occluded to closed transition is not the reverse of the forward transition. The contact E18-S49 in the occluded structure persists until the sliding of the M20 loop is nearly complete Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P0ABQ4
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