3.A.2.2.1
H+-translocating V-type ATPase. The 3-D structure is known (Lau and Rubinstein, 2012). More recently, Zhou and Sazanov 2019 solved cryo-EM structures of the intact Thermus thermophilus V/A-ATPase in three rotational
states with two substates. These structures indicate substantial
flexibility between V1 and Vo in a working enzyme,
which results from mechanical competition between central shaft
rotation and resistance from the peripheral stalks.
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| Accession Number: | Q56403 |
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| Protein Name: | V-type ATP synthase alpha chain |
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| Length: | 578 |
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| Molecular Weight: | 63632.00 |
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| Species: | Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) [300852] |
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| Substrate |
hydron |
|---|
1: MIQGVIQKIA GPAVIAKGML GARMYDICKV GEEGLVGEII RLDGDTAFVQ VYEDTSGLKV
61: GEPVVSTGLP LAVELGPGML NGIYDGIQRP LERIREKTGI YITRGVVVHA LDREKKWAWT
121: PMVKPGDEVR GGMVLGTVPE FGFTHKILVP PDVRGRVKEV KPAGEYTVEE PVVVLEDGTE
181: LKMYHTWPVR RARPVQRKLD PNTPFLTGMR ILDVLFPVAM GGTAAIPGPF GSGKTVTQQS
241: LAKWSNADVV VYVGCGERGN EMTDVLVEFP ELTDPKTGGP LMHRTVLIAN TSNMPVAARE
301: ASIYVGVTIA EYFRDQGFSV ALMADSTSRW AEALREISSR LEEMPAEEGY PPYLAARLAA
361: FYERAGKVIT LGGEEGAVTI VGAVSPPGGD MSEPVTQSTL RIVGAFWRLD ASLAFRRHFP
421: AINWNGSYSL FTSALDPWYR ENVAEDYPEL RDAISELLQR EAGLQEIVQL VGPDALQDAE
481: RLVIEVGRII REDFLQQNAY HEVDAYCSMK KAYGIMKMIL AFYKEAEAAI KRGVSIDEIL
541: QLPVLERIGR ARYVSEEEFP AYFEEAMKEI QGAFKALA