News Column

Reports from Max-Planck-Institute for Medical Research Highlight Recent Findings in Molecular Motors

May 13, 2014



By a News Reporter-Staff News Editor at Life Science Weekly -- Fresh data on Molecular Motors are presented in a new report. According to news originating from Heidelberg, Germany, by NewsRx correspondents, research stated, "ATPases of the AAA+ superfamily are large oligomeric molecular machines that remodel their substrates by converting the energy from ATP hydrolysis into mechanical force. This study focuses on the molecular chaperone ClpB, the bacterial homologue of Hsp104, which reactivates aggregated proteins under cellular stress conditions."

Our news journalists obtained a quote from the research from Max-Planck-Institute for Medical Research, "Based on high-resolution crystal structures in different nucleotide states, mutational analysis and nucleotide-binding kinetics experiments, the ATPase cycle of the C-terminal nucleotide-binding domain (NBD2), one of the motor subunits of this AAA+ disaggregation machine, is dissected mechanistically. The results provide insights into nucleotide sensing, explaining how the conserved sensor 2 motif contributes to the discrimination between ADP and ATP binding. Furthermore, the role of a conserved active-site arginine (Arg621), which controls binding of the essential Mg2+ ion, is described. Finally, a hypothesis is presented as to how the ATPase activity is regulated by a conformational switch that involves the essential Walker A lysine."

According to the news editors, the research concluded: "In the proposed model, an unusual side-chain conformation of this highly conserved residue stabilizes a catalytically inactive state, thereby avoiding unnecessary ATP hydrolysis."

For more information on this research see: Elements in nucleotide sensing and hydrolysis of the AAA+ disaggregation machine ClpB: a structure-based mechanistic dissection of a molecular motor. Acta Crystallographica Section D, Biological Crystallography, 2014;70(Pt 2):582-95 (see also Molecular Motors).

The news correspondents report that additional information may be obtained from C. Zeymer, Dept. of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Jahnstrasse 29, 69120 Heidelberg, Germany. Additional authors for this research include T.R. Barends, N.D. Werbeck, I. Schlichting and J. Reinstein.

Keywords for this news article include: Europe, Germany, Heidelberg, Nanotechnology, Molecular Motors, Emerging Technologies.

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Source: Life Science Weekly