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      Recent advances in the structural biology of the 26S proteasome.

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          Abstract

          There is growing appreciation for the fundamental role of structural dynamics in the function of macromolecules. In particular, the 26S proteasome, responsible for selective protein degradation in an ATP dependent manner, exhibits dynamic conformational changes that enable substrate processing. Recent cryo-electron microscopy (cryo-EM) work has revealed the conformational dynamics of the 26S proteasome and established the function of the different conformational states. Technological advances such as direct electron detectors and image processing algorithms allowed resolving the structure of the proteasome at atomic resolution. Here we will review those studies and discuss their contribution to our understanding of proteasome function.

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          Author and article information

          Journal
          Int. J. Biochem. Cell Biol.
          The international journal of biochemistry & cell biology
          Elsevier BV
          1878-5875
          1357-2725
          October 2016
          : 79
          Affiliations
          [1 ] Department of Molecular Structural Biology, Max Planck institute of Biochemistry, 82152, Martinsried, Germany.
          [2 ] Department of Molecular Structural Biology, Max Planck institute of Biochemistry, 82152, Martinsried, Germany. Electronic address: sakata@biochem.mpg.de.
          Article
          S1357-2725(16)30217-5
          10.1016/j.biocel.2016.08.008
          27498189
          8bbc83a5-2d02-42a8-83a3-f505e66cead8
          History

          Cryoelectron microscopy,AAA+ ATPase,26S proteasome,Single particle analysis,Structural biology

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