Two-step ATP-driven opening of cohesin head (2/3).

2017. Two-step ATP-driven opening of cohesin head (2/3).
Positioning of Smc1A-K1120. Molecular Dynamics. After ATP hydrolysis at active site 1 of human cohesin, aminoacid Smc1A-K1120 moves close to the catalytic water molecule in the active site 2 and remained in its new location in a stable conformation.
Published in: Scientific Reports 7, 3266. [ https://www.nature.com/articles/s4159...]

Two-step ATP-driven opening of cohesin head (2/3). severin
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