ATP Synthase b Subunit Dimerization DomainATP Synthase b Subunit Dimerization Domain

Structural highlights

1l2p is a 1 chain structure with sequence from Escherichia coli. The December 2005 RCSB PDB Molecule of the Month feature on ATP Synthase by David S. Goodsell is 10.2210/rcsb_pdb/mom_2005_12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.55Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ATPF_ECOLI 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).[1] Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0) (By similarity).[2]

Evolutionary Conservation

 

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. McCormick KA, Cain BD. Targeted mutagenesis of the b subunit of F1F0 ATP synthase in Escherichia coli: Glu-77 through Gln-85. J Bacteriol. 1991 Nov;173(22):7240-8. PMID:1682301
  2. McCormick KA, Cain BD. Targeted mutagenesis of the b subunit of F1F0 ATP synthase in Escherichia coli: Glu-77 through Gln-85. J Bacteriol. 1991 Nov;173(22):7240-8. PMID:1682301

1l2p, resolution 1.55Å

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