title: A thermostable enzyme as an experimental platform to study properties of less stable homologues.
abstract: The structural and functional characterization of proteins is frequently hampered by lack of stability or by insufficient assembly of oligomeric proteins in over-expression systems. Using F(1)-ATPase as a case study, we tackled this problem by introducing function-determining domains from a difficult-to-handle variety of an enzyme into a stable homologue.
authors.affiliation: Department of Structural Biology, Faculty of Earth and Life Science, De Boelelaan 1085, 1081 HV Amsterdam, The Netherlands.
authors.forename: Holger
authors.initials: H
authors.lastname: Lill
authors.forename: Toru
authors.initials: T
authors.lastname: Hisabori
authors.forename: Georg
authors.initials: G
authors.lastname: Groth
authors.forename: Dirk
authors.initials: D
authors.lastname: Bald
mesh_terms: D000595:Amino Acid Sequence; D002736:Chloroplasts / Q000378:metabolism; D004795:Enzyme Stability; D004798:Enzymes / Q000737:chemistry*; D006358:Hot Temperature; D007700:Kinetics; D008928:Mitochondria / Q000737:chemistry; D008954:Models, Biological; D008969:Molecular Sequence Data; D010940:Plant Proteins / Q000737:chemistry; D011487:Protein Conformation; D015202:Protein Engineering / Q000379:methods*; D011506:Proteins / Q000737:chemistry; D006180:Proton-Translocating ATPases / Q000737:chemistry*; D011993:Recombinant Fusion Proteins / Q000737:chemistry; D017386:Sequence Homology, Amino Acid; D013379:Substrate Specificity; D013696:Temperature
chemical_list: D004798:Enzymes; D010940:Plant Proteins; D011506:Proteins; D011993:Recombinant Fusion Proteins; D006180:Proton-Translocating ATPases