1. Evidence for the Existence of Elaborate Enzyme Complexes in the Paleoarchean Era
- Author
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Sandra Schlee, Veronika Schmid, Rainer Merkl, Reinhard Sterner, Linn Carstensen, Josef M. Sperl, Samuel Blanquart, Bernd Reisinger, Alexandra Holinski, Chitra Rajendran, Institut für Biophysik und physikalische Biochemie, Universität Regensburg (UR), Bioinformatics and Sequence Analysis (BONSAI), Laboratoire d'Informatique Fondamentale de Lille (LIFL), Université de Lille, Sciences et Technologies-Institut National de Recherche en Informatique et en Automatique (Inria)-Université de Lille, Sciences Humaines et Sociales-Centre National de la Recherche Scientifique (CNRS)-Université de Lille, Sciences et Technologies-Institut National de Recherche en Informatique et en Automatique (Inria)-Université de Lille, Sciences Humaines et Sociales-Centre National de la Recherche Scientifique (CNRS)-Inria Lille - Nord Europe, and Institut National de Recherche en Informatique et en Automatique (Inria)
- Subjects
Models, Molecular ,Protein Folding ,Protein subunit ,Substrate channeling ,Allosteric regulation ,Crystallography, X-Ray ,Extinction, Biological ,Biochemistry ,Protein Structure, Secondary ,Catalysis ,Evolution, Molecular ,Colloid and Surface Chemistry ,Protein structure ,Aminohydrolases ,Multienzyme Complexes ,biology ,Chemistry ,Last universal ancestor ,Active site ,General Chemistry ,Archaea ,[SDV.BIBS]Life Sciences [q-bio]/Quantitative Methods [q-bio.QM] ,biology.protein ,Protein folding ,Salt bridge ,[INFO.INFO-BI]Computer Science [cs]/Bioinformatics [q-bio.QM] - Abstract
International audience; : Due to the lack of macromolecular fossils, the enzymatic repertoire of extinct species has remained largely unknown to date. In an attempt to solve this problem, we have characterized a cyclase subunit (HisF) of the imidazole glycerol phosphate synthase (ImGP-S), which was reconstructed from the era of the last universal common ancestor of cellular organisms (LUCA). As observed for contemporary HisF proteins, the crystal structure of LUCA-HisF adopts the (βα)8-barrel architecture, one of the most ancient folds. Moreover, LUCA-HisF (i) resembles extant HisF proteins with regard to internal 2-fold symmetry, active site residues, and a stabilizing salt bridge cluster, (ii) is thermostable and shows a folding mechanism similar to that of contemporary (βα)8-barrel enzymes, (iii) displays high catalytic activity, and (iv) forms a stable and functional complex with the glutaminase subunit (HisH) of an extant ImGP-S. Furthermore, we show that LUCA-HisF binds to a reconstructed LUCA-HisH protein with high affinity. Our findings suggest that the evolution of highly efficient enzymes and enzyme complexes has already been completed in the LUCA era, which means that sophisticated catalytic concepts such as substrate channeling and allosteric communication existed already 3.5 billion years ago.
- Published
- 2013