(PDF) Conformational Heterogeneity Within the LID Domain

Conformational Heterogeneity Within the LID Domain Mediates Substrate Binding to Escherichia Coli Adenylate Kinase: Function Follows Fluctuations

Topics in Current Chemistry - Germany

doi 10.1007/128_2012_410

Full Text

Abstract

Available in full text

Categories

Date

January 1, 2013

Authors

Travis P. Schrank

Vincent J. Hilser

Publisher

Springer Berlin Heidelberg

Related search

Substrate Binding Specifically Modulates Domain Arrangements in Adenylate Kinase

Biophysical Journal

English

E. Coli Adenylate Kinase Exhibits Inter-Domain Coupling

Biophysical Journal

English

Adenylate Energy Charge in Escherichia Coli CR341T28 and Properties of Heat-Sensitive Adenylate Kinase.

Journal of Bacteriology

Molecular Biology

English

Exploring Structural Motifs Necessary for Substrate Binding in the Active Site of Escherichia Coli Pantothenate Kinase

Bioorganic and Medicinal Chemistry

Organic Chemistry

Molecular Medicine

Molecular Biology

Clinical Biochemistry

Pharmaceutical Science

English

Adenylate Kinase-Independent Thiamine Triphosphate Accumulation Under Severe Energy Stress in Escherichia Coli

BMC Microbiology

English

Molecular Dynamics of Apo-Adenylate Kinase: A Distance Replica Exchange Method for the Free Energy of Conformational Fluctuations

Journal of Physical Chemistry B

Theoretical Chemistry

Materials Chemistry

English

A Mechanism of Covalent Substrate Binding in the X-Ray Structure of Subunit K of the Escherichia Coli Dihydroxyacetone Kinase

Proceedings of the National Academy of Sciences of the United States of America

Multidisciplinary

English

Escherichia Coli Dihydroxyacetone Kinase Controls Gene Expression by Binding to Transcription Factor DhaR

Molecular Biology

English

Lid Conformational Dynamics and Substrate Specificity of the Pili Constructing Sortase C Enzymes

Biophysical Journal

English