Researchers reveal structure and function of a molecularmotor
) data set and built nucleotide models. Note that labels shown as ‘ATP’ refer to ATPγS, which has been used for structure determination. ‘apo’ labels refer to discontinuous densities within the nucleotide binding pockets. ‘ADP*’ notation refers to [ADP + Mg]. All cryo-EM densities are shown at the same isosurface threshold. b, Table listing the nucleotides in the RuvB nucleotide binding pockets according to the RuvB subunit/cluster and the RuvB motor state.
Extended Data Fig. 9 Opening and closing motions of the RuvB nucleotide binding pocket at the inter-subunit interface during the nucleotide cycle. a, cryo-EM density and corresponding atomic models of inter-subunit interfaces of the nucleotide binding pockets in RuvB. The cryo-EM densities have been contoured at the same threshold level . Residues contributing to ATP-binding and ATP hydrolysis are shown in stick representation.
a, Side-by-side comparison of the atomic models corresponding to the RuvB motors states in the nucleotide cycle and the initiation states obtained from dataset t2. b, A hydrophobic interaction of RuvAis established with α -helix α3 and the presensor-1 β hairpin of RuvB subunit D or E. Surface representation of RuvB with hydrophilic amino acids shown in turquoise and hydrophobic residues shown in sepia. A cartoon model of only one RuvAbinding interface highlighting the wedge-like effect.
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