title: How to Compare, Analyze, and Morph Between Crystal Structures of Different Conformations: The P-Type ATPase Example.
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.
authors.affiliation: Department of Molecular Biology and Genetics, Aarhus University, Gustav Wieds Vej 10c, Aarhus C, 8000, Denmark. jelka@mbg.au.dk.
authors.forename: Jesper L
authors.initials: JL
authors.lastname: Karlsen
authors.affiliation: Department of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK.
authors.forename: Maike
authors.initials: M
authors.lastname: Bublitz
mesh_terms: D000251:Adenosine Triphosphatases / Q000737:chemistry* / Q000378:metabolism; D055162:Biocatalysis; D019295:Computational Biology / Q000379:methods*; D018360:Crystallography, X-Ray; D030562:Databases, Protein; D004583:Electrons; D004795:Enzyme Stability; D008958:Models, Molecular; D011487:Protein Conformation
chemical_list: D000251:Adenosine Triphosphatases
keywords: Conformational states; Metal fluorides; Morphing; P-Type ATPase structure