2RQ7

Solution structure of the epsilon subunit chimera combining the N-terminal beta-sandwich domain from T. Elongatus bp-1 f1 and the C-terminal alpha-helical domain from spinach chloroplast F1

Summary for 2RQ7

• Entry DOI: 10.2210/pdb2rq7/pdb
• Related: 2RQ6
• Descriptor: ATP synthase epsilon chain,ATP synthase epsilon chain, chloroplastic (1 entity in total)
• Functional Keywords: atp synthase, f1fo atp synthase, f1-atpase, epsilon subunit, chloroplast, atp synthesis, cf1, hydrogen ion transport, hydrolase, ion transport, membrane, thylakoid, transport, plastid, cf(1)
• Biological source: Thermosynechococcus elongatus (strain BP-1); More
• Total number of polymer chains: 1
• Total formula weight: 14602.53

Authors

Yagi, H.,Konno, H.,Murakami-Fuse, T.,Oroguchi, H.,Akutsu, T.,Ikeguchi, M.,Hisabori, T. (deposition date: 2009-03-03, release date: 2010-01-12, Last modification date: 2024-05-01)

Primary citation

Yagi, H.,Konno, H.,Murakami-Fuse, T.,Isu, A.,Oroguchi, T.,Akutsu, H.,Ikeguchi, M.,Hisabori, T.
Structural and functional analysis of the intrinsic inhibitor subunit epsilon of F1-ATPase from photosynthetic organisms.
Biochem.J., 425:85-94, 2010

PubMed Abstract: The epsilon subunit, a small subunit located in the F1 domain of ATP synthase and comprising two distinct domains, an N-terminal beta-sandwich structure and a C-terminal alpha-helical region, serves as an intrinsic inhibitor of ATP hydrolysis activity. This inhibitory function is especially important in photosynthetic organisms as the enzyme cannot synthesize ATP in the dark, but may catalyse futile ATP hydrolysis reactions. To understand the structure-function relationship of this subunit in F1 from photosynthetic organisms, we solved the NMR structure of the epsilon subunit of ATP synthase obtained from the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1, and examined the flexibility of the C-terminal domains using molecular dynamics simulations. In addition, we revealed the significance of the C-terminal alpha-helical region of the epsilon subunit in determining the binding affinity to the complex based on the assessment of the inhibition of ATPase activity by the cyanobacterial epsilon subunit and the chimaeric subunits composed of the N-terminal domain from the cyanobacterium and the C-terminal domain from spinach. The differences observed in the structural and biochemical properties of chloroplast and bacterial epsilon subunits explains the distinctive characteristics of the epsilon subunits in the ATPase complex of the photosynthetic organism.

PubMed: 19785575
DOI: 10.1042/BJ20091247

Experimental method

SOLUTION NMR