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Verfasst von:Meier, Sebastian [VerfasserIn]   i
 Holstein, Thomas W. [VerfasserIn]   i
 Özbek, Suat [VerfasserIn]   i
Titel:Continuous Molecular Evolution of Protein-Domain Structures by Single Amino Acid Changes
Verf.angabe:Sebastian Meier, Pernille R. Jensen, Charles N. David, Jarrod Chapman, Thomas W. Holstein, Stephan Grzesiek, Suat Özbek
Umfang:6 S.
Fussnoten:Gesehen am 08.05.2017
Titel Quelle:Enthalten in: Current biology
Jahr Quelle:2007
Band/Heft Quelle:17(2007), 2, S. 173-178
ISSN Quelle:1879-0445
Abstract:Summary Protein structures cluster into families of folds that can result from extremely different amino acid sequences [1]. Because the enormous amount of genetic information generates a limited number of protein folds [2], a particular domain structure often assumes numerous functions. How new protein structures and new functions evolve under these limitations remains elusive. Molecular evolution may be driven by the ability of biomacromolecules to adopt multiple conformations as a bridge between different folds [3-6]. This could allow proteins to explore new structures and new tasks while part of the structural ensemble retains the initial conformation and function as a safeguard [7]. Here we show that a global structural switch can arise from single amino acid changes in cysteine-rich domains (CRD) of cnidarian nematocyst proteins. The ability of these CRDs to form two structures with different disulfide patterns from an identical cysteine pattern is distinctive [8]. By applying a structure-based mutagenesis approach, we demonstrate that a cysteine-rich domain can interconvert between two natively occurring domain structures via a bridge state containing both structures. Comparing cnidarian CRD sequences leads us to believe that the mutations we introduced to stabilize each structure reflect the birth of new protein folds in evolution.
DOI:doi:10.1016/j.cub.2006.10.063
URL:Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.

Kostenfrei: Verlag: http://dx.doi.org/10.1016/j.cub.2006.10.063
 Kostenfrei: Verlag: http://www.sciencedirect.com/science/article/pii/S0960982206024444
 DOI: https://doi.org/10.1016/j.cub.2006.10.063
Datenträger:Online-Ressource
Sprache:eng
K10plus-PPN:1558292659
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