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

2013 ◽  
pp. 95-121 ◽  
Author(s):  
Travis P. Schrank ◽  
James O. Wrabl ◽  
Vincent J. Hilser
Keyword(s):  
Escherichia Coli ◽  
Adenylate Kinase ◽  
Substrate Binding ◽  
Conformational Heterogeneity ◽  
Lid Domain

scholarly journals Molecular Dynamics Studies on the Conformational Transitions of Adenylate Kinase: A Computational Evidence for the Conformational Selection Mechanism

2013 ◽  
Vol 2013 ◽  
pp. 1-7 ◽  
Author(s):  
Jie Ping ◽  
Pei Hao ◽  
Yi-Xue Li ◽  
Jing-Fang Wang
Keyword(s):  
Escherichia Coli ◽  
Molecular Dynamics ◽  
Adenylate Kinase ◽  
Large Scale ◽  
Conformational Transition ◽  
Conformational Transitions ◽  
Selection Mechanism ◽  
Conformational Selection ◽  
Domain Motion ◽  
Lid Domain

Escherichia coliadenylate kinase (ADK) is a monomeric phosphotransferase enzyme that catalyzes reversible transfer of phosphoryl group from ATP to AMP with a large-scale domain motion. The detailed mechanism for this conformational transition remains unknown. In the current study, we performed long time-scale molecular dynamics simulations on both open and closed states of ADK. Based on the structural analyses of the simulation trajectories, we detected over 20 times conformational transitions between the open and closed states of ADK and identified two novel conformations as intermediate states in the catalytic processes. With these findings, we proposed a possible mechanism for the large-scale domain motion ofEscherichia coliADK and its catalytic process: (1) the substrate free ADK adopted an open conformation; (2) ATP bound with LID domain closure; (3) AMP bound with NMP domain closure; (4) phosphoryl transfer occurred with ATP, and AMP converted into two ADPs, and no conformational transition was detected in the enzyme; (5) LID domain opened with one ADP released; (6) another ADP released with NMP domain open. As both open and closed states sampled a wide range of conformation transitions, our simulation strongly supported the conformational selection mechanism forEscherichia coliADK.

Contributions of the substrate-binding arginine residues to maleate-induced closure of the active site of Escherichia coli aspartate aminotransferase

2001 ◽  
Vol 268 (6) ◽  
pp. 1640-1645
Author(s):  
Annelise Matharu ◽  
Hideyuki Hayashi ◽  
Hiroyuki Kagamiyama ◽  
Bruno Maras ◽  
Robert A. John
Keyword(s):  
Escherichia Coli ◽  
Active Site ◽  
Aspartate Aminotransferase ◽  
Substrate Binding ◽  
Arginine Residues

scholarly journals Circular dichroism investigation of Escherichia coli adenylate kinase.

1987 ◽  
Vol 262 (6) ◽  
pp. 2502-2506
Author(s):  
M. Monnot ◽  
A.M. Gilles ◽  
I.S. Girons ◽  
S. Michelson ◽  
O. Bârzu ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Circular Dichroism ◽  
Adenylate Kinase ◽  
Circular Dichroïsm

scholarly journals Substitution of a serine residue for proline-87 reduces catalytic activity and increases susceptibility to proteolysis of Escherichia coli adenylate kinase.

1986 ◽  
Vol 83 (16) ◽  
pp. 5798-5802 ◽  
Author(s):  
A. M. Gilles ◽  
I. Saint-Girons ◽  
M. Monnot ◽  
S. Fermandjian ◽  
S. Michelson ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Catalytic Activity ◽  
Adenylate Kinase ◽  
Serine Residue

scholarly journals Structural and catalytic properties of a deletion derivative (delta 133-157) of Escherichia coli adenylate kinase

1991 ◽  
Vol 266 (17) ◽  
pp. 10781-10786
Author(s):  
T. Rose ◽  
M. Brune ◽  
A. Wittinghofer ◽  
K. Le Blay ◽  
W.K. Surewicz ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Adenylate Kinase ◽  
Catalytic Properties ◽  
Deletion Derivative
Sign in / Sign up

Export Citation Format

Share Document