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Structural basis for a unique ATP synthase core complex from nanoarcheaum equitans

Authors :
Mohanty, S.
Jobichen, C.
Chichili, V. P. R.
Velázquez-Campoy, Adrián
Low, B.C.
Hogue, C. W. V.
Sivaraman, J.
Mohanty, S.
Jobichen, C.
Chichili, V. P. R.
Velázquez-Campoy, Adrián
Low, B.C.
Hogue, C. W. V.
Sivaraman, J.
Publication Year :
2015

Abstract

Background: Structural asymmetry upon nucleotide binding is crucial for catalytic activity of ATP synthases. Results: The structures of apo and bound A3B3 hexamer of N. equitans ATP synthase show conformational inflexibility. Conclusion: The N. equitans A3B3 hexamer is an inactive form. Significance: The structure of inactive form of N. equitans ATP synthase A3B3 is shown for the first time.

Details

Database :
OAIster
Notes :
English
Publication Type :
Electronic Resource
Accession number :
edsoai.on1104789264
Document Type :
Electronic Resource

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