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: | P07677 |
Protein Name: | ATP synthase subunit beta |
Length: | 473 |
Molecular Weight: | 51938.00 |
Species: | Bacillus sp. (strain PS3) [2334] |
Location1 / Topology2 / Orientation3: |
Cell membrane1 / Peripheral membrane protein2 |
Substrate |
hydron |
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1: MTRGRVIQVM GPVVDVKFEN GHLPAIYNAL KIQHKARNEN EVDIDLTLEV ALHLGDDTVR
61: TIAMASTDGL IRGMEVIDTG APISVPVGQV TLGRVFNVLG EPIDLEGDIP ADARRDPIHR
121: PAPKFEELAT EVEILETGIK VVDLLAPYIK GGKIGLFGGA GVGKTVLIQE LIHNIAQEHG
181: GISVFAGVGE RTREGNDLYH EMKDSGVISK TAMVFGQMNE PPGARMRVAL TGLTMAEYFR
241: DEQGQDGLLF IDNIFRFTQA GSEVSALLGR MPSAIGYQPT LATEMGQLQE RITSTAKGSI
301: TSIQAIYVPA DDYTDPAPAT TFSHLDATTN LERKLAEMGI YPAVDPLVST SRALAPEIVG
361: EEHYQVARKV QQTLERYKEL QDIIAILGMD ELSDEDKLVV HRARRIQFFL SQNFHVAEQF
421: TGQPGSYVPV KETVRGFKEI LEGKYDHLPE DRFRLVGRIE EVVEKAKAMG VEV