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4mjn

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Structure of the c ring of the CF1FO ATP synthases.

Structural highlights

4mjn is a 14 chain structure with sequence from Triticum aestivum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 6Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ATPH_WHEAT F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation (By similarity). Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of between 10-14 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits (By similarity).

Publication Abstract from PubMed

In eukaryotic and prokaryotic cells, F-ATP synthases provide energy through the synthesis of ATP. The chloroplast F-ATP synthase (CF1FO-ATP synthase) of plants is integrated into the thylakoid membrane via its FO-domain subunits a, b, b' and c Subunit c with a stoichiometry of 14 and subunit a form the gate for H(+)-pumping, enabling the coupling of electrochemical energy with ATP synthesis in the F1 sector.Here we report the crystallization and structure determination of the c14-ring of subunit c of the CF1FO-ATP synthase from spinach chloroplasts. The crystals belonged to space group C2, with unit-cell parameters a=144.420, b=99.295, c=123.51 A, and beta=104.34 degrees and diffracted to 4.5 A resolution. Each c-ring contains 14 monomers in the asymmetric unit. The length of the c-ring is 60.32 A, with an outer ring diameter 52.30 A and an inner ring width of 40 A.

Crystallographic structure of the turbine C-ring from spinach chloroplast F-ATP synthase.,Balakrishna AM, Seelert H, Marx SH, Dencher NA, Gruber G Biosci Rep. 2014 Apr 1;34(2). pii: BSR20130114. doi: 10.1042/BSR20130114. Print, 2014 Apr 1. PMID:27919036^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Balakrishna AM, Seelert H, Marx SH, Dencher NA, Gruber G. Crystallographic structure of the turbine C-ring from spinach chloroplast F-ATP synthase. Biosci Rep. 2014 Apr 1;34(2). pii: BSR20130114. doi: 10.1042/BSR20130114. Print, 2014 Apr 1. PMID:27919036 doi:http://dx.doi.org/10.1042/BSR20130114