NDLI: Converting conformational changes to electrostatic energy in molecular motors: The energetics of ATP synthase

Content Provider	PubMed Central
Author	Marek, S̆trajbl Avital, Shurki Warshel, Arieh
Copyright Year	2003
Abstract	F1-ATPase is the catalytic component of the ATP synthase molecular machine responsible for most of the uphill synthesis of ATP in living systems. The enormous advances in biochemical and structural studies of this machine provide an opportunity for detailed understanding of the nature of its rotary mechanism. However, further quantitative progress in this direction requires development of reliable ways of translating the observed structural changes to the corresponding energies. This requirement is particularly challenging because we are dealing with a large system that couples major structural changes with a chemical process. The present work provides such a structure–function correlation by using the linear response approximation to describe the rotary mechanism. This approach allows one to evaluate the energy of transitions between different conformational states by considering only the changes in the corresponding electrostatic energies of the ligands. The relevant energetics are also obtained by calculating the linear response approximation-based free energies of transferring the ligands from water to the different sites of F1-ATPase in their different conformational states. We also use the empirical valence bond approach to evaluate the actual free-energy profile for the ATP synthesis in the different conformational states of the system. Integrating the information from the different approaches provides a semiquantitative structure–function correlation for F1-ATPase. It is found that the conformational changes are converted to changes in the electrostatic interaction between the protein and its ligands, which drives the ATP synthesis.
Related Links	http://dx.doi.org/10.1073/pnas.2436328100
Ending Page	14839
Page Count	6
Starting Page	14834
File Format	PDF
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	25
Volume Number	100
Language	English
Publisher	National Academy of Sciences
Publisher Date	2003-12-09
Access Restriction	Open
Rights Holder	National Academy of Sciences
Subject Keyword	General Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Converting conformational changes to electrostatic energy in molecular motors: The energetics of ATP synthase.

Large conformational changes of the ɛ subunit in the bacterial F1F0 ATP synthase provide a ratchet action to regulate this rotary motor enzyme

Energy-dependent conformational changes in the epsilon subunit of the chloroplast ATP synthase (CF0CF1).

Electrostatic origin of the unidirectionality of walking myosin V motors

From ATP synthase dimers to C-ring conformational changes: unified model of the mitochondrial permeability transition pore

ATP synthase: From sequence to ring size to the P/O ratio

Resistance of Akt kinases to dephosphorylation through ATP-dependent conformational plasticity

CONFORMATIONAL CHANGES IN MYOSIN B AND ACTOMYOSIN INDUCED BY ATP *

ATP-induced conformational changes in the restriction endonuclease from Escherichia coli K-12.

Converting conformational changes to electrostatic energy in molecular motors: The energetics of ATP synthase

Similar Documents

Converting conformational changes to electrostatic energy in molecular motors: The energetics of ATP synthase.

Large conformational changes of the ɛ subunit in the bacterial F1F0 ATP synthase provide a ratchet action to regulate this rotary motor enzyme

Energy-dependent conformational changes in the epsilon subunit of the chloroplast ATP synthase (CF0CF1).

Electrostatic origin of the unidirectionality of walking myosin V motors

From ATP synthase dimers to C-ring conformational changes: unified model of the mitochondrial permeability transition pore

ATP synthase: From sequence to ring size to the P/O ratio

Resistance of Akt kinases to dephosphorylation through ATP-dependent conformational plasticity

CONFORMATIONAL CHANGES IN MYOSIN B AND ACTOMYOSIN INDUCED BY ATP *

ATP-induced conformational changes in the restriction endonuclease from Escherichia coli K-12.

Converting conformational changes to electrostatic energy in molecular motors: The energetics of ATP synthase