A thermostable enzyme as an experimental platform to study properties of less stable homologues.
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.
Lill
Holger
H
Department of Structural Biology, Faculty of Earth and Life Science, De Boelelaan 1085, 1081 HV Amsterdam, The Netherlands.
Hisabori
Toru
T
Groth
Georg
G
Bald
Dirk
D
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
D004798:Enzymes; D010940:Plant Proteins; D011506:Proteins; D011993:Recombinant Fusion Proteins; D006180:Proton-Translocating ATPases