Solution structure of the 45-residue magnesium ATP-binding peptide of adenylate kinase as examined by 2-D NMR, FTIR, and CD spectroscopy

Biochemistry ◽  
1988 ◽  
Vol 27 (10) ◽  
pp. 3588-3598 ◽  
Author(s):  
David C. Fry ◽  
D. Michael Byler ◽  
Heino Susi ◽  
Eleanor M. Brown ◽  
Stephen A. Kuby ◽  
...  
Keyword(s):  
Adenylate Kinase ◽  
Solution Structure ◽  
Cd Spectroscopy ◽  
Atp Binding ◽  
Binding Peptide

Solution Structure and Function in Trifluoroethanol of PP-50, an ATP-Binding Peptide from F1ATPase

1995 ◽  
Vol 319 (1) ◽  
pp. 110-122 ◽  
Author(s):  
W.J. Chuang ◽  
C. Abeygunawardana ◽  
A.G. Gittis ◽  
P.L. Pedersen ◽  
A.S. Mildvan
Keyword(s):  
Solution Structure ◽  
Structure And Function ◽  
Atp Binding ◽  
Binding Peptide ◽  
And Function

scholarly journals Structural and Functional Characterization of RecG Helicase under Dilute and Molecular Crowding Conditions

2012 ◽  
Vol 2012 ◽  
pp. 1-8
Author(s):  
Sarika Saxena ◽  
Satoru Nagatoishi ◽  
Daisuke Miyoshi ◽  
Naoki Sugimoto
Keyword(s):  
Functional Characterization ◽  
Cd Spectroscopy ◽  
Helical Conformation ◽  
Atp Binding ◽  
Molecular Crowding ◽  
Active Structure ◽  
Dna Junctions ◽  
Unique Protein

In an ATP-dependent reaction, theEscherichia coliRecG helicase unwinds DNA junctionsin vitro. We present evidence of a unique protein conformational change in the RecG helicase from anα-helix to aβ-strand upon an ATP binding under dilute conditions using circular dichroism (CD) spectroscopy. In contrast, under molecular crowding conditions, theα-helical conformation was stable even upon an ATP binding. These distinct conformational behaviors were observed to be independent of Na+and Mg2+. Interestingly, CD measurements demonstrated that the spectra of a frayed duplex decreased with increasing of the RecG concentration both under dilute and molecular crowding conditions in the presence of ATP, suggesting that RecG unwound the frayed duplex. Our findings raise the possibility that theα-helix andβ-strand forms of RecG are a preactive and an active structure with the helicase activity, respectively.

NMR Solution Structure of a Complex of Calmodulin with a Binding Peptide of the Ca2+Pump†,‡

Biochemistry ◽  
1999 ◽  
Vol 38 (38) ◽  
pp. 12320-12332 ◽  
Author(s):  
Bettina Elshorst ◽  
Mirko Hennig ◽  
Holger Försterling ◽  
Alexander Diener ◽  
Marcus Maurer ◽  
...  
Keyword(s):  
Solution Structure ◽  
Nmr Solution Structure ◽  
Binding Peptide

scholarly journals Tracking the ATP-binding response in adenylate kinase in real time

2021 ◽  
Vol 7 (47) ◽  
Author(s):  
Fredrik Orädd ◽  
Harsha Ravishankar ◽  
Jack Goodman ◽  
Per Rogne ◽  
Lars Backman ◽  
...  
Keyword(s):  
Real Time ◽  
Adenylate Kinase ◽  
Atp Binding

scholarly journals Solution Structure of the Conserved Hypothetical Protein Rv2302 from Mycobacterium tuberculosis

2006 ◽  
Vol 188 (16) ◽  
pp. 5993-6001 ◽  
Author(s):  
Garry W. Buchko ◽  
Chang-Yub Kim ◽  
Thomas C. Terwilliger ◽  
Michael A. Kennedy
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Solution Structure ◽  
Hydrophobic Interactions ◽  
Hypothetical Protein ◽  
Cd Spectroscopy ◽  
Size Exclusion ◽  
Correlation Spectrum ◽  
Nuclear Overhauser ◽  
Α Helix ◽  
Β Sheet

ABSTRACT The Mycobacterium tuberculosis protein Rv2302 (80 residues; molecular mass of 8.6 kDa) has been characterized using nuclear magnetic resonance (NMR) and circular dichroism (CD) spectroscopy. While the biochemical function of Rv2302 is still unknown, recent microarray analyses show that Rv2302 is upregulated in response to starvation and overexpression of heat shock proteins and, consequently, may play a role in the biochemical processes associated with these events. Rv2302 is a monomer in solution as shown by size exclusion chromatography and NMR spectroscopy. CD spectroscopy suggests that Rv2302 partially unfolds upon heating and that this unfolding is reversible. Using NMR-based methods, the solution structure of Rv2302 was determined. The protein contains a five-strand, antiparallel β-sheet core with one C-terminal α-helix (A61 to A75) nestled against its side. Hydrophobic interactions between residues in the α-helix and β-strands 3 and 4 hold the α-helix near the β-sheet core. The electrostatic potential on the solvent-accessible surface is primarily negative with the exception of a positive arginine pocket composed of residues R18, R70, and R74. Steady-state {1H}-15N heteronuclear nuclear Overhauser effects indicate that the protein's core is rigid on the picosecond timescale. The absence of amide cross-peaks for residues G13 to H19 in the 1H-15N heteronuclear single quantum correlation spectrum suggests that this region, a loop between β-strands 1 and 2, undergoes motion on the millisecond to microsecond timescale. Dali searches using the structure closest to the average structure do not identify any high similarities to any other known protein structure, suggesting that the structure of Rv2302 may represent a novel protein fold.

An ATP-Binding Peptide

1973 ◽  
Vol 37 (0) ◽  
pp. 121-125 ◽  
Author(s):  
G. Barany ◽  
R. B. Merrifield
Keyword(s):  
Atp Binding ◽  
Binding Peptide
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