The c 15  ring of the  Spirulina platensis  F‐ATP synthase: F 1 /F 0  symmetry mismatch is not obligatory | Zendy

Pogoryelov Denys | Zendy; Yu Jinshu | Zendy; Meier Thomas | Zendy; Vonck Janet | Zendy; Dimroth Peter | Zendy; Muller Daniel J | Zendy

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The c 15 ring of the Spirulina platensis F‐ATP synthase: F 1 /F 0 symmetry mismatch is not obligatory

Author(s) -

Pogoryelov Denys,

Yu Jinshu,

Meier Thomas,

Vonck Janet,

Dimroth Peter,

Muller Daniel J

Publication year - 2005

Publication title -

embo reports

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 4.584

H-Index - 184

eISSN - 1469-3178

pISSN - 1469-221X

DOI - 10.1038/sj.embor.7400517

Subject(s) - atp synthase , spirulina (dietary supplement) , ring (chemistry) , monomer , protein subunit , crystallography , chemistry , carboxylate , stereochemistry , enzyme , biochemistry , polymer , organic chemistry , raw material , gene

The oligomeric c ring of the F‐ATP synthase from the alkaliphilic cyanobacterium Spirulina platensis was isolated and characterized. Mass spectroscopy analysis indicated a mass of 8,210 Da, reflecting that of a c monomer. The mass increased by 206 Da after treatment with the c‐subunit‐specific inhibitor dicyclohexylcarbodiimide (DCCD), which indicated modification of the ion‐binding carboxylate by DCCD. Atomic force microscopy topographs of c rings from S. platensis showed 15 symmetrically assembled subunits. The c 15 ‐mer reported here is the largest c ring that is isolated and does not show the classical c‐ring mismatch to the three‐fold symmetry of the F 1 domain.

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