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P-Type ATPases pp 523–539Cite as

How to Compare, Analyze, and Morph Between Crystal Structures of Different Conformations: The P-Type ATPase Example

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Part of the book series: Methods in Molecular Biology ((MIMB,volume 1377))

Abstract

In the past 15 years, a large body of structural information on P-type ATPases has accumulated in the Protein Data Bank. The available crystal structures cover different enzymes in a variety of conformational states that are associated with the enzymatic activity of ATP-dependent ion translocation across membranes. This chapter provides an overview about the available structural information, along with some practical instructions on how to make meaningful comparisons of structures in different conformations, and how to generate morphs between series of structures, in order to analyze domain movements and structural flexibility.

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Authors and Affiliations

  1. Department of Molecular Biology and Genetics, Aarhus University, Gustav Wieds Vej 10c, Aarhus C, 8000, Denmark

    Jesper L. Karlsen

  2. Department of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK

    Maike Bublitz

Authors
  1. Jesper L. Karlsen
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  2. Maike Bublitz
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Correspondence to Jesper L. Karlsen .

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Editors and Affiliations

  1. Department of Biochemistry, Biocenter, University of Oxford, Oxford, Oxfordshire, United Kingdom

    Maike Bublitz

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Karlsen, J.L., Bublitz, M. (2016). How to Compare, Analyze, and Morph Between Crystal Structures of Different Conformations: The P-Type ATPase Example. In: Bublitz, M. (eds) P-Type ATPases. Methods in Molecular Biology, vol 1377. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-3179-8_43

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  • DOI: https://doi.org/10.1007/978-1-4939-3179-8_43

  • Publisher Name: Humana Press, New York, NY

  • Print ISBN: 978-1-4939-3178-1

  • Online ISBN: 978-1-4939-3179-8

  • eBook Packages: Springer Protocols

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