Artículos de revistas
Correlated Inter-Domain Motions in Adenylate Kinase
Fecha
2014-07Registro en:
Esteban Martin, Santiago; Fenwick, Robert Bryn ; Ådén, Jörgen ; Cossins, Benjamin ; Bertoncini, Carlos Walter; et al.; Correlated Inter-Domain Motions in Adenylate Kinase; Public Library Of Science; Plos Computational Biology; 10; 7; 7-2014; 1-7
1553-734X
Autor
Esteban Martin, Santiago
Fenwick, Robert Bryn
Ådén, Jörgen
Cossins, Benjamin
Bertoncini, Carlos Walter
Guallar, Victor
Wolf Watz, Magnus
Salvatella, Xavier
Resumen
Correlated inter-domain motions in proteins can mediate fundamental biochemical processes such as signal transduction and allostery. Here we characterize at structural level the inter-domain coupling in a multidomain enzyme, Adenylate Kinase (AK), using computational methods that exploit the shape information encoded in residual dipolar couplings (RDCs) measured under steric alignment by nuclear magnetic resonance (NMR). We find experimental evidence for a multi-state equilibrium distribution along the opening/closing pathway of Adenylate Kinase, previously proposed from computational work, in which inter-domain interactions disfavour states where only the AMP binding domain is closed. In summary, we provide a robust experimental technique for study of allosteric regulation in AK and other enzymes.