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Your search keyword '"Salla I. Virtanen"' showing total 2 results
Start Over Author "Salla I. Virtanen" Publisher mdpi ag
2 results on '"Salla I. Virtanen"'

1. The Convergence of the Hedgehog/Intein Fold in Different Protein Splicing Mechanisms

Author

Hannes M. Beyer, Salla I. Virtanen, A. Sesilja Aranko, Kornelia M. Mikula, George T. Lountos, Alexander Wlodawer, O. H. Samuli Ollila, and Hideo Iwaï

Subjects
protein-splicing mechanism, intein, protein engineering, protein evolution, protease, Biology (General), QH301-705.5, Chemistry, QD1-999
Abstract

Protein splicing catalyzed by inteins utilizes many different combinations of amino-acid types at active sites. Inteins have been classified into three classes based on their characteristic sequences. We investigated the structural basis of the protein splicing mechanism of class 3 inteins by determining crystal structures of variants of a class 3 intein from Mycobacterium chimaera and molecular dynamics simulations, which suggested that the class 3 intein utilizes a different splicing mechanism from that of class 1 and 2 inteins. The class 3 intein uses a bond cleavage strategy reminiscent of proteases but share the same Hedgehog/INTein (HINT) fold of other intein classes. Engineering of class 3 inteins from a class 1 intein indicated that a class 3 intein would unlikely evolve directly from a class 1 or 2 intein. The HINT fold appears as structural and functional solution for trans-peptidyl and trans-esterification reactions commonly exploited by diverse mechanisms using different combinations of amino-acid types for the active-site residues.

Published
2020
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2. The Convergence of the Hedgehog/Intein Fold in Different Protein Splicing Mechanisms

Author

George T. Lountos, Hideo Iwaï, Hannes M. Beyer, Kornelia M. Mikula, O. H. Samuli Ollila, Alexander Wlodawer, Salla I. Virtanen, A. Sesilja Aranko, Institute of Biotechnology, Biochemistry and Biotechnology, Biophysical chemistry, and University Management

Subjects
0301 basic medicine, STRUCTURAL BASIS, Proteases, PARTICLE MESH EWALD, RNA Splicing, Computational biology, Molecular Dynamics Simulation, DATA-COLLECTION, intein, Article, Catalysis, FULLY-AUTOMATIC CHARACTERIZATION, Inteins, Mycobacterium, Protein evolution, Inorganic Chemistry, lcsh:Chemistry, 03 medical and health sciences, Bacterial Proteins, DOMAIN, Protein splicing, CHYMOTRYPSIN, Catalytic Domain, Protein Splicing, Hedgehog Proteins, CRYSTAL-STRUCTURE, Physical and Theoretical Chemistry, protein evolution, Molecular Biology, Hedgehog, lcsh:QH301-705.5, Spectroscopy, 030102 biochemistry & molecular biology, REFINEMENT, Chemistry, Organic Chemistry, protein-splicing mechanism, protein engineering, protease, General Medicine, Protein engineering, EVOLUTION, Computer Science Applications, 030104 developmental biology, lcsh:Biology (General), lcsh:QD1-999, RNA splicing, 1182 Biochemistry, cell and molecular biology, Intein
Abstract

Protein splicing catalyzed by inteins utilizes many different combinations of amino-acid types at active sites. Inteins have been classified into three classes based on their characteristic sequences. We investigated the structural basis of the protein splicing mechanism of class 3 inteins by determining crystal structures of variants of a class 3 intein from Mycobacterium chimaera and molecular dynamics simulations, which suggested that the class 3 intein utilizes a different splicing mechanism from that of class 1 and 2 inteins. The class 3 intein uses a bond cleavage strategy reminiscent of proteases but share the same Hedgehog/INTein (HINT) fold of other intein classes. Engineering of class 3 inteins from a class 1 intein indicated that a class 3 intein would unlikely evolve directly from a class 1 or 2 intein. The HINT fold appears as structural and functional solution for trans-peptidyl and trans-esterification reactions commonly exploited by diverse mechanisms using different combinations of amino-acid types for the active-site residues.

Published
2020

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