ArticleNature structural & molecular biology2011
A metal switch for controlling the activity of molecular motor proteins.
Article in Nature structural & molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 15 citations in OpenAlex.
- Direct Effects of Toxic Divalent Cations on Contractile Proteins with Implications for the Heart: Unraveling Mechanisms of Dysfunction.International journal of molecular sciences · 2023Review
- PCSK9 as a Target for Development of a New Generation of Hypolipidemic Drugs.Molecules (Basel, Switzerland) · 2022Review
- Crystal structure of SARS-CoV-2 nsp10 bound to nsp14-ExoN domain reveals an exoribonuclease with both structural and functional integrity.Nucleic acids research · 2021Article
- Switch-1 instability at the active site decouples ATP hydrolysis from force generation in myosin II.Cytoskeleton (Hoboken, N.J.) · 2021Article
- From isolated structures to continuous networks: A categorization of cytoskeleton-based motile engineered biological microstructures.Wiley interdisciplinary reviews. Nanomedicine and nanobiotechnology · 2019Review
- Characterization of kinesin switch I mutations that cause hereditary spastic paraplegia.PloS one · 2017Article
- Kinesin Motor Enzymology: Chemistry, Structure, and Physics of Nanoscale Molecular Machines.Biophysical reviews · 2015Article
- Remote control of myosin and kinesin motors using light-activated gearshifting.Nature nanotechnology · 2014Article
- 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 · 2014Article
- Metal switch-controlled myosin II from Dictyostelium discoideum supports closure of nucleotide pocket during ATP binding coupled to detachment from actin filaments.The Journal of biological chemistry · 2013Article
- Magnesium impacts myosin V motor activity by altering key conformational changes in the mechanochemical cycle.Biochemistry · 2013Article
- Engineered, harnessed, and hijacked: synthetic uses for cytoskeletal systems.Trends in cell biology · 2012Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Kinesins are molecular motors that require a divalent metal ion (for example, Mg(2+)) to convert the energy of ATP hydrolysis into directed force production along microtubules. Here we present the crystal structure of a recombinant kinesin motor domain bound to Mn(2+) and ADP and report on a serine-to-cysteine substitution in the switch 1 motif of kinesin that allows its ATP hydrolysis activity to be controlled by adjusting the ratio of Mn(2+) to Mg(2+). This mutant kinesin binds ATP similarly in the presence of either metal ion, but its ATP hydrolysis activity is greatly diminished in the presence of Mg(2+). In human kinesin-1 and kinesin-5 as well as Drosophila melanogaster kinesin-10 and kinesin-14, this defect is rescued by Mn(2+), providing a way to control both the enzymatic activity and force-generating ability of these nanomachines.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.