Kinetic stabilisation of a modular protein by domain interactions
Open Access
- 30 October 1998
- journal article
- Published by Wiley in FEBS Letters
- Vol. 438 (1-2) , 127-130
- https://doi.org/10.1016/s0014-5793(98)01287-3
Abstract
Protein S, a two‐domain spore coat protein from Myxococcus xanthus, is structurally related to eye‐lens βγ‐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.Keywords
This publication has 23 references indexed in Scilit:
- Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genesPublished by Elsevier ,2004
- Kinetic studies of β-sheet protein foldingCurrent Opinion in Structural Biology, 1998
- Mutational analysis of hydrophobic domain interactions in γB-crystallin from bovine eye lensProtein Science, 1997
- The domains in γb-crystallin: identical fold-different stabilitiesJournal of Molecular Biology, 1997
- Extremely rapid protein folding in the absence of intermediatesNature Structural & Molecular Biology, 1995
- NMR-derived three-dimensional solution structure of protein S complexed with calciumStructure, 1994
- The evolution of lenticular proteins: The β- and γ-crystallin super gene familyProgress in Biophysics and Molecular Biology, 1988
- Myxococcus xanthus spore coat protein S may have a similar structure to vertebrate lens βγ-crystallinsNature, 1985
- Myxobacteria: Cell Interactions, Genetics, and DevelopmentAnnual Review of Microbiology, 1979
- Nucleation, Rapid Folding, and Globular Intrachain Regions in ProteinsProceedings of the National Academy of Sciences, 1973