3.A.2.1.14 The H+-translocating ATP synthase, Atp(Unc)ABCDEFGH. The 3-D structure has been determined by cryo-EM (Guo et al. 2019). The position of subunit epsilon shows how it is able to inhibit ATP hydrolysis while allowing ATP synthesis. The architecture of the membrane region shows how the ATP synthase is able to perform the same core functions as the equivalent, but more complicated, mitochondrial complex. The structures reveal the path of transmembrane proton translocation and provide a model for understanding decades of biochemical analysis, interrogating the roles of specific residues in the enzyme (Guo et al. 2019).
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Accession Number: | P09218 |
Protein Name: | ATP synthase subunit a |
Length: | 238 |
Molecular Weight: | 26590.00 |
Species: | Bacillus sp. (strain PS3) [2334] |
Number of TMSs: | 5 |
Location1 / Topology2 / Orientation3: |
Cell membrane1 / Multi-pass membrane protein2 |
Substrate |
hydron |
---|
1: MEHKAPLVEF LGLTFNLSDM LMITITCLIV FIIAVAATRS LQLRPTGMQN FMEWVFDFVR
61: GIINSTMDWQ TGGRFLTLGV TLIMYVFVAN MLGLPFSVHV NGELWWKSPT ADATVTLTLA
121: VMVVALTHYY GVKMKGASDY LRDYTRPVAW LFPLKIIEEF ANTLTLGLRL FGNIYAGEIL
181: LGLLASLGTH YGVLGAVGAS QFPIMVWQAF SIFVGTIQAF IFTMLTMVYM AHKVSHDH