Kinetic stabilisation of a modular protein by domain interactions.
Protein S, a two-domain spore coat protein from Myxococcus xanthus, is structurally related to eye-lens Pr crystallins. No natural monomeric one-domain member of this protein superfamily is known. To determine the stability of the single domains and to explain the ubiquitous domain duplication, the isolated domains of protein S were constructed. The N-domain is thermodynamically more stable than the C-domain. In intact protein S, domain interactions lead to an apparent decrease in stability of the N-terminal domain, whereas the C-terminal domain is stabilised. In contrast, unfolding kinetics of both domains are decreased 100-fold due to interactions in the complete molecule.
Wenk
M
M
Institut für Biophysik und Physikalische Biochemie, Universität Regensburg, Germany.
Jaenicke
R
R
Mayr
E M
EM
D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D002118:Calcium / Q000378:metabolism; D002152:Calorimetry, Differential Scanning; D002942:Circular Dichroism; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000235:genetics; D007700:Kinetics; D005810:Multigene Family; D016941:Myxococcus xanthus / Q000737:chemistry*; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000302:isolation & purification; D013050:Spectrometry, Fluorescence; D013816:Thermodynamics
D001426:Bacterial Proteins; C046032:Myxococcus spore coat proteins; D011993:Recombinant Fusion Proteins; D002118:Calcium