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Showing 1–8 of 8 results
Advanced filters: Author: Kutti R. Vinothkumar Clear advanced filters

  • Complex I is the first enzyme of the mitochondrial electron transport chain and it is essential for oxidative phosphorylation in mammalian mitochondria; here the electron cryo-microscopy structure of complex I from bovine heart mitochondria is reported, advancing knowledge of its structure in mammals.

    • Kutti R. Vinothkumar
    • Jiapeng Zhu
    • Judy Hirst
    Research
    Nature
    Volume: 515, P: 80-84

  • Pannexins are large pore channels involved in ion and ATP release. Here the authors use cryo-EM structures of Pannexins 1 and 3 to demonstrate the effects of distinct residue substitutions on channel structure and function.

    • Nazia Hussain
    • Ashish Apotikar
    • Aravind Penmatsa
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-14

  • The bacterial enzyme PaaZ is involved in the breakdown of environmental pollutants via the aerobic-anaerobic hybrid pathway but its substrate transfer mechanism is not fully understood. Here, the authors present cryoEM structures of free and ligand-bound PaaZ that suggest a mechanism for internal substrate channeling.

    • Nitish Sathyanarayanan
    • Giuseppe Cannone
    • Kutti R. Vinothkumar
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-12

  • Electron cryomicroscopy structures are provided for all core and supernumerary protein subunits of mammalian complex I, a 45-subunit enzyme that powers eukaryotic respiration.

    • Jiapeng Zhu
    • Kutti R. Vinothkumar
    • Judy Hirst
    Research
    Nature
    Volume: 536, P: 354-358

  • McrBC is a bacterial antiphage defense system that cleaves methylated DNA and is composed of the AAA+ GTPase motor McrB and the endonuclease McrC. Here, the authors present the cryo-EM structure of E. coli McrBC that reveals how McrC inserts a stalk-like structure into the pore of the ring-shaped McrB hexamer and discuss mechanistic implications.

    • Neha Nirwan
    • Yuzuru Itoh
    • Kayarat Saikrishnan
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-9

  • Porins, like OmpG, are embedded in the outer membrane of bacteria and facilitate uptake and secretion of nutrients and ions. Here the authors present a protocol for solid state NMR structure determination of proteins larger than 25 kDa and use it to structurally characterize membrane embedded OmpG.

    • Joren S. Retel
    • Andrew J. Nieuwkoop
    • Hartmut Oschkinat
    ResearchOpen Access
    Nature Communications
    Volume: 8, P: 1-10

  • Many challenges and considerations must be evaluated when expanding and supporting new cryo-electron microscopy facilities.

    • Kutti R. Vinothkumar
    Comments & Opinion
    Nature Methods
    Volume: 18, P: 437-438