Artículo
Local frustration around enzyme active sites
Freiberger, Maria Ines; Guzovsky, Ana Brenda
; Wolynes, Peter G.; Parra, Rodrigo Gonzalo
; Ferreiro, Diego
Fecha de publicación:
02/2019
Editorial:
National Academy of Sciences
Revista:
Proceedings of the National Academy of Sciences of The United States of America
ISSN:
0027-8424
e-ISSN:
1091-6490
Idioma:
Inglés
Tipo de recurso:
Artículo publicado
Clasificación temática:
Resumen
Conflicting biological goals often meet in the specification of protein sequences for structure and function. Overall, strong energetic conflicts are minimized in folded native states according to the principle of minimal frustration, so that a sequence can spontaneously fold, but local violations of this principle open up the possibility to encode the complex energy landscapes that are required for active biological functions. We survey the local energetic frustration patterns of all protein enzymes with known structures and experimentally annotated catalytic residues. In agreement with previous hypotheses, the catalytic sites themselves are often highly frustrated regardless of the protein oligomeric state, overall topology, and enzymatic class. At the same time a secondary shell of more weakly frustrated interactions surrounds the catalytic site itself. We evaluate the conservation of these energetic signatures in various family members of major enzyme classes, showing that local frustration is evolutionarily more conserved than the primary structure itself.
Palabras clave:
BIOINFORMATICS
,
CATALYTIC SITES
,
EVOLUTION
,
LOCAL FRUSTRATION
,
PROTEIN ENZYMES
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Licencia
Identificadores
Colecciones
Articulos(IQUIBICEN)
Articulos de INSTITUTO DE QUIMICA BIOLOGICA DE LA FACULTAD DE CS. EXACTAS Y NATURALES
Articulos de INSTITUTO DE QUIMICA BIOLOGICA DE LA FACULTAD DE CS. EXACTAS Y NATURALES
Citación
Freiberger, Maria Ines; Guzovsky, Ana Brenda; Wolynes, Peter G.; Parra, Rodrigo Gonzalo; Ferreiro, Diego; Local frustration around enzyme active sites; National Academy of Sciences; Proceedings of the National Academy of Sciences of The United States of America; 116; 10; 2-2019; 4037-4043
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