Structural Basis of Mechanochemical Coupling in a Hexameric Molecular Motor
作者： Erika J. Mancini , Jelena Telenius , Jiří Lísal , Jonathan M. Grimes , Dennis H. Bamford
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摘要: The P4 protein of bacteriophage φ 12 is a hexameric molecular motor closely related to superfamily 4 helicases. converts chemical energy from ATP hydrolysis into mechanical work, translocate single-stranded RNA viral capsid. basis mechanochemical coupling, i.e. how small ∼1 A changes in the ATP-binding site are amplified nanometer scale motion along nucleic acid, not understood at atomic level. Here we study detail coupling using structural and biochemical analyses mutants. We show that conserved region, consisting helicase motifs H3 H4 loop L2, constitutes moving lever motor. tip encompasses an RNA-binding moves reaction coordinate. flanked by γ-phosphate sensors (Asn-234 Ser-252) report nucleotide state neighboring subunits control position. Insertion arginine finger (Arg-279) catalytic concomitant with movement commences hydrolysis. This ensures cooperative sequential tightly coupled motion. Given conservation, mutated residues may play similar roles other helicases motors. © 2008 American Society for Biochemistry Molecular Biology, Inc.
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R.Ian Menz, John E. Walker, Andrew G.W. Leslie, Structure of Bovine Mitochondrial F1-ATPase with Nucleotide Bound to All Three Catalytic Sites: Implications for the Mechanism of Rotary Catalysis Cell. ,vol. 106, pp. 331- 341 ,(2001) , 10.1016/S0092-8674(01)00452-4
Kiyonobu Karata, Takabumi Inagawa, Anthony J. Wilkinson, Takashi Tatsuta, Teru Ogura, Dissecting the role of a conserved motif (the second region of homology) in the AAA family of ATPases. Site-directed mutagenesis of the ATP-dependent protease FtsH. Journal of Biological Chemistry. ,vol. 274, pp. 26225- 26232 ,(1999) , 10.1074/JBC.274.37.26225
Markus Dittrich, Klaus Schulten, PcrA Helicase, a Prototype ATP-Driven Molecular Motor Structure. ,vol. 14, pp. 1345- 1353 ,(2006) , 10.1016/J.STR.2006.06.017
Erika J. Mancini, Denis E. Kainov, Jonathan M. Grimes, Roman Tuma, Dennis H. Bamford, David I. Stuart, Atomic Snapshots of an RNA Packaging Motor Reveal Conformational Changes Linking ATP Hydrolysis to RNA Translocation Cell. ,vol. 118, pp. 743- 755 ,(2004) , 10.1016/J.CELL.2004.09.007
Markus Dittrich, Shigehiko Hayashi, Klaus Schulten, ATP Hydrolysis in the βTP and βDP Catalytic Sites of F1-ATPase Biophysical Journal. ,vol. 87, pp. 2954- 2967 ,(2004) , 10.1529/BIOPHYSJ.104.046128
Emmanuel Skordalakes, James M. Berger, Structural insights into RNA-dependent ring closure and ATPase activation by the Rho termination factor. Cell. ,vol. 127, pp. 553- 564 ,(2006) , 10.1016/J.CELL.2006.08.051
Randall M. Story, Thomas A. Steitz, Structure of the recA protein–ADP complex Nature. ,vol. 355, pp. 374- 376 ,(1992) , 10.1038/355374A0
Satoshi Soga, Takato Noumi, Michiyasu Takeyama, Masatomo Maeda, Masamitsu Futai, Mutational replacements of conserved amino acid residues in the α subunit change the catalytic properties of Escherichia coli F1-ATPase Archives of Biochemistry and Biophysics. ,vol. 268, pp. 643- 648 ,(1989) , 10.1016/0003-9861(89)90332-9
Dahai Gai, Rui Zhao, Dawei Li, Carla V. Finkielstein, Xiaojiang S. Chen, Mechanisms of conformational change for a replicative hexameric helicase of SV40 large tumor antigen Cell. ,vol. 119, pp. 47- 60 ,(2004) , 10.1016/J.CELL.2004.09.017
Chao Lin, Paul R Caron, Joseph L Kim, Kurt A Morgenstern, James P Griffith, Maureen D Dwyer, John A Thomson, Mark A Murcko, Hepatitis C virus NS3 RNA helicase domain with a bound oligonucleotide: the crystal structure provides insights into the mode of unwinding Structure. ,vol. 6, pp. 89- 100 ,(1998) , 10.1016/S0969-2126(98)00010-0