2YN1

Crystal Structure of Ancestral Thioredoxin Relative to Last Gamma- Proteobacteria Common Ancestor (LGPCA) from the Precambrian Period

Summary for 2YN1

• Entry DOI: 10.2210/pdb2yn1/pdb
• Related: 2YJ7 2YNX 2YOI 2YPM 3ZIV 4BA7
• Descriptor: LGPCA THIOREDOXIN, TRIETHYLENE GLYCOL (3 entities in total)
• Functional Keywords: oxidoreductase, alpha beta, electron transport, ancestral reconstructed protein
• Biological source: SYNTHETIC CONSTRUCT
• Total number of polymer chains: 2
• Total formula weight: 23749.36

Authors

Gavira, J.A.,Ingles-Prieto, A.,Ibarra-Molero, B.,Sanchez-Ruiz, J.M. (deposition date: 2012-10-11, release date: 2013-08-21, Last modification date: 2023-12-20)

Primary citation

Ingles-Prieto, A.,Ibarra-Molero, B.,Delgado-Delgado, A.,Perez-Jimenez, R.,Fernandez, J.M.,Gaucher, E.A.,Sanchez-Ruiz, J.M.,Gavira, J.A.
Conservation of Protein Structure Over Four Billion Years
Structure, 21:1690-, 2013

PubMed Abstract: 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.

PubMed: 23932589
DOI: 10.1016/J.STR.2013.06.020

Experimental method

X-RAY DIFFRACTION (1.3 Å)