ATP-hydrolysis-associated conformational change of the ?-subunit during the rotation of F(1)-ATPase (F(1)) has been discussed using cryo-electron microscopy (cryo-EM). Since it is worthwhile to further investigate the conformation of ATP at the catalytic subunit through an alternative approach, the structure of ATP bound to the F(1)?-subunit monomer (?) was analyzed by solid-state NMR. The adenosine conformation of ATP-? was similar to that of ATP analog in F(1) crystal structures. ^(31)P...
[NMR paper] Solid-state NMR chemical shift analysis for determining the conformation of ATP bound to Na,K-ATPase in its native membrane
Solid-state NMR chemical shift analysis for determining the conformation of ATP bound to Na,K-ATPase in its native membrane
Structures of membrane proteins determined by X-ray crystallography and, increasingly, by cryo-electron microscopy often fail to resolve the structural details of unstable or reactive small molecular ligands in their physiological sites. This work demonstrates that ^(13)C chemical shifts measured by magic-angle spinning (MAS) solid-state NMR (SSNMR) provide unique information on the conformation of a labile ligand in the physiological site of a functional protein in...
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Structural Insight into an Alzheimer’s Brain-Derived Spherical Assembly of Amyloid ? by Solid-State NMR
Structural Insight into an Alzheimer’s Brain-Derived Spherical Assembly of Amyloid ? by Solid-State NMR
Sudhakar Parthasarathy, Masafumi Inoue, Yiling Xiao, Yoshitaka Matsumura, Yo-ichi Nabeshima, Minako Hoshi and Yoshitaka Ishii
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.5b03373/20150518/images/medium/ja-2015-03373k_0004.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.5b03373
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/IQmUqF-Pq1k
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05-19-2015 09:10 AM
[NMR paper] Structural Insight into an Alzheimer's Brain-Derived Spherical Assembly of Amyloid ? by Solid-state NMR.
Structural Insight into an Alzheimer's Brain-Derived Spherical Assembly of Amyloid ? by Solid-state NMR.
Related Articles Structural Insight into an Alzheimer's Brain-Derived Spherical Assembly of Amyloid ? by Solid-state NMR.
J Am Chem Soc. 2015 May 4;
Authors: Parthasarathy S, Inoue M, Xiao Y, Matsumura Y, Nabeshima YI, Hoshi M, Ishii Y
Abstract
Accumulating evidence suggests that various neurodegenerative diseases, including Alzheimer's disease (AD), are linked to cytotoxic diffusible aggregates of amyloid proteins, which are...
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05-06-2015 11:59 AM
[NMR paper] Monitoring ATP hydrolysis and ATPase inhibitor screening using (1)H NMR.
Monitoring ATP hydrolysis and ATPase inhibitor screening using (1)H NMR.
Related Articles Monitoring ATP hydrolysis and ATPase inhibitor screening using (1)H NMR.
Chem Commun (Camb). 2014 Aug 29;
Authors: Guo B, Gurel PS, Shu R, Higgs HN, Pellegrini M, Mierke DF
Abstract
We present a versatile method to characterize ATPase and kinase activities and discover new inhibitors of these proteins. The proton NMR-based assay directly monitors ATP turnover and is easy to implement, requires no additional reagents and can potentially be...
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08-30-2014 11:00 PM
NMR analysis of the {alpha}IIb{beta}3 cytoplasmic interaction suggests a mechanism for integrin regulation [Biochemistry]
NMR analysis of the {alpha}IIb{beta}3 cytoplasmic interaction suggests a mechanism for integrin regulation
Metcalf, D. G., Moore, D. T., Wu, Y., Kielec, J. M., Molnar, K., Valentine, K. G., Wand, A. J., Bennett, J. S., DeGrado, W. F....
Date: 2010-12-28
The integrin IIbβ3 is a transmembrane (TM) heterodimeric adhesion receptor that exists in equilibrium between resting and active ligand binding conformations. In resting IIbβ3, the TM and cytoplasmic domains of IIb and β3 form a heterodimer that constrains IIbβ3 in its resting conformation. To study the structure...
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12-29-2010 06:01 AM
Structure analysis of membrane-reconstituted subunit c-ring of E. coli H+-ATP synthase by solid-state NMR.
Structure analysis of membrane-reconstituted subunit c-ring of E. coli H+-ATP synthase by solid-state NMR.
Structure analysis of membrane-reconstituted subunit c-ring of E. coli H+-ATP synthase by solid-state NMR.
J Biomol NMR. 2010 Sep;48(1):1-11
Authors: Todokoro Y, Kobayashi M, Sato T, Kawakami T, Yumen I, Aimoto S, Fujiwara T, Akutsu H
The subunit c-ring of H(+)-ATP synthase (F(o) c-ring) plays an essential role in the proton translocation across a membrane driven by the electrochemical potential. To understand its structure and function, we...
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12-18-2010 12:00 PM
NMR analysis of the {alpha}IIb{beta}3 cytoplasmic interaction suggests a mechanism for integrin regulation.
NMR analysis of the {alpha}IIb{beta}3 cytoplasmic interaction suggests a mechanism for integrin regulation.
NMR analysis of the {alpha}IIb{beta}3 cytoplasmic interaction suggests a mechanism for integrin regulation.
Proc Natl Acad Sci U S A. 2010 Dec 14;
Authors: Metcalf DG, Moore DT, Wu Y, Kielec JM, Molnar K, Valentine KG, Wand AJ, Bennett JS, Degrado WF
The integrin ?IIb?3 is a transmembrane (TM) heterodimeric adhesion receptor that exists in equilibrium between resting and active ligand binding conformations. In resting ?IIb?3, the TM and...
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12-16-2010 09:21 PM
[NMR paper] Structural insight into human Zn(2+)-bound S100A2 from NMR and homology modeling.
Structural insight into human Zn(2+)-bound S100A2 from NMR and homology modeling.
Related Articles Structural insight into human Zn(2+)-bound S100A2 from NMR and homology modeling.
Biochem Biophys Res Commun. 2001 Oct 26;288(2):462-7
Authors: Randazzo A, Acklin C, Schäfer BW, Heizmann CW, Chazin WJ
The S100 subfamily of EF-hand proteins is distinguished by the binding of Zn(2+) in addition to Ca(2+). In an effort to understand the role of Zn(2+) in modulating the activity of S100 proteins, we have carried out heteronuclear NMR studies of...
Structural analysis of ATP bound to the F(1)-ATPase beta-subunit monomer by solid-state NMR- insight into the hydrolysis mechanism in F(1)
Linear Mode
