PMID:22066536
| Citation |
Liao, JC (2011) Mechanical transduction mechanisms of RecA-like molecular motors. J. Biomol. Struct. Dyn. 29:497-507 |
|---|---|
| Abstract |
A majority of ATP-dependent molecular motors are RecA-like proteins, performing diverse functions in biology. These RecA-like molecular motors consist of a highly conserved core containing the ATP-binding site. Here I examined how ATP binding within this core is coupled to the conformational changes of different RecA-like molecular motors. Conserved hydrogen bond networks and conformational changes revealed two major mechanical transduction mechanisms: (1) intra-domain conformational changes and (2) inter-domain conformational changes. The intra-domain mechanism has a significant hydrogen bond rearrangement within the domain containing the P-loop, causing relative motion between two parts of the protein. The inter-domain mechanism exhibits little conformational change in the P-loop domain. Instead, the major conformational change is observed between the P-loop domain and an adjacent domain or subunit containing the arginine finger. These differences in the mechanical transduction mechanisms may link to the underlying energy surface governing a Brownian ratchet or a power stroke. |
| Links |
PubMed Online version:10.1080/07391102.2011.10507401 |
| Keywords |
Adenosine Triphosphate/metabolism; Binding Sites; Energy Metabolism; Hydrogen Bonding; Models, Molecular; Molecular Motor Proteins/chemistry; Molecular Motor Proteins/metabolism; Movement; Protein Conformation; Protein Structure, Tertiary; Rec A Recombinases/chemistry; Rec A Recombinases/metabolism |
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