Identifying Sequential Substrate Binding at the Single-Molecule Level by Enzyme Mechanical Stabilization-Reference-Cited by-同舟云学术

Identifying Sequential Substrate Binding at the Single-Molecule Level by Enzyme Mechanical Stabilization

Published:2015-04-13 Issue:4 Volume:9 Page:3996-4005
ISSN:1936-0851
Container-title:ACS Nano
language:en
Short-container-title:ACS Nano

Author:

Rivas-Pardo Jaime Andrés¹²,Alegre-Cebollada Jorge¹,Ramírez-Sarmiento César A.²,Fernandez Julio M.¹,Guixé Victoria²

Affiliation:

1. Department of Biological Sciences, Columbia University, Northwest Corner Building, 550 West 120 Street, New York, New York 10027, United States

2. Laboratorio de Bioquímica y Biología Molecular, Departamento de Biología, Facultad de Ciencias, Universidad de Chile, Las Palmeras 3425, Casilla 653, Santiago, Chile

Funder

National Institute of Allergy and Infectious Diseases

Ministerio de Educación, Gobierno de Chile

Division of Biological Infrastructure

Fondo Nacional de Desarrollo Científico y Tecnológico

National Heart, Lung, and Blood Institute

Comisión Nacional de Investigación Científica y Tecnológica

Publisher

American Chemical Society (ACS)

Subject

General Physics and Astronomy,General Engineering,General Materials Science

Link

https://pubs.acs.org/doi/pdf/10.1021/nn507480v

Reference54 articles.

1. The intrinsic dynamics of enzymes plays a dominant role in determining the structural changes induced upon inhibitor binding

2. Induced fit on sugar binding activates ribokinase

3. Substrate Binding Drives Large-Scale Conformational Changes in the Hsp90 Molecular Chaperone

4. A Spring-loaded Release Mechanism Regulates Domain Movement and Catalysis in Phosphoglycerate Kinase

5. Domain Motions and Quaternary Packing of Phosphofructokinase-2 from Escherichia coli Studied by Small Angle X-ray Scattering and Homology Modeling

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