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: | P09219 |
Protein Name: | ATP synthase subunit alpha |
Length: | 502 |
Molecular Weight: | 54591.00 |
Species: | Bacillus sp. (strain PS3) [2334] |
Location1 / Topology2 / Orientation3: |
Cell membrane1 / Peripheral membrane protein2 |
Substrate |
hydron |
---|
1: MSIRAEEISA LIKQQIENYE SQIQVSDVGT VIQVGDGIAR AHGLDNVMSG EAVEFANAVM
61: GMALNLEENN VGIVILGPYT GIKEGDEVRR TGRIMEVPVG ETLIGRVVNP LGQPVDGLGP
121: VETTETRPIE SRAPGVMDRR SVHEPLQTGI KAIDALVPIG RGQRELIIGD RQTGKTSVAI
181: DTIINQKDQN MICIYVAIGQ KESTVATVVE TLAKHGAPDY TIVVTASASQ PAPLLFLAPY
241: AGVAMGEYFM IMGKHVLVVI DDLSKQAAAY RQLSLLLRRP PGREAYPGDI FYLHSRLLER
301: AAKLSDAKGG GSLTALPFVE TQAGDISAYI PTNVISITDG QIFLQSDLFF SGVRPAINAG
361: LSVSRVGGAA QIKAMKKVAG TLRLDLAAYR ELEAFAQFGS DLDKATQANV ARGARTVEVL
421: KQDLHQPIPV EKQVLIIYAL TRGFLDDIPV EDVRRFEKEF YLWLDQNGQH LLEHIRTTKD
481: LPNEDDLNQA IEAFKKTFVV SQ