Conservation of Protein Structure over Four Billion Years

Little is known about the evolution of protein structures and the degree of protein structure conservation over planetary time scales. Here, we report the X-ray crystal structures of seven laboratory resurrections of Precambrian thioredoxins dating up to approximately four billion years ago. Despite...

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Bibliographic Details
Published in:Structure (London) 2013-09, Vol.21 (9), p.1690-1697
Main Authors: Ingles-Prieto, Alvaro, Ibarra-Molero, Beatriz, Delgado-Delgado, Asuncion, Perez-Jimenez, Raul, Fernandez, Julio M., Gaucher, Eric A., Sanchez-Ruiz, Jose M., Gavira, Jose A.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Archaeal Proteins - chemistry
Conservation
Conserved Sequence
Crystal structure
Crystallography, X-Ray
Dating
Escherichia coli Proteins - chemistry
Evolution
Evolution, Molecular
Humans
Hydrogen Bonding
Models, Molecular
Phylogeny
Planetary evolution
Protein Structure, Secondary
Protein Structure, Tertiary
Proteins
Structural Homology, Protein
Thioredoxins - chemistry
Time
X-rays
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Summary:Little is known about the evolution of protein structures and the degree of protein structure conservation over planetary time scales. Here, we report the X-ray crystal structures of seven laboratory resurrections of Precambrian thioredoxins dating up to approximately four billion years ago. Despite considerable sequence differences compared with extant enzymes, the ancestral proteins display the canonical thioredoxin fold, whereas only small structural changes have occurred over four billion years. This remarkable degree of structure conservation since a time near the last common ancestor of life supports a punctuated-equilibrium model of structure evolution in which the generation of new folds occurs over comparatively short periods and is followed by long periods of structural stasis. [Display omitted] •3D structure determination reliably extended to approximately four billion years ago•Ancestral and derived structural features in extant proteins readily identified•Remarkable degree of structure conservation back to a time close to the origin of life•Illustration of a powerful approach to explore the evolution of protein structures Ingles-Prieto et al. report structures for seven resurrected Precambrian thioredoxins dating back to about four billion years ago. Despite considerable sequence differences compared with extant enzymes, the ancestral proteins display the canonical fold and reveal a remarkable degree of structure conservation.
ISSN:0969-2126
1878-4186
DOI:10.1016/j.str.2013.06.020