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.
|
Accession Number: | Q56404 |
Protein Name: | V-type ATP synthase beta chain |
Length: | 478 |
Molecular Weight: | 53160.00 |
Species: | Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) [300852] |
Substrate |
hydron |
---|
1: MDLLKKEYTG ITYISGPLLF VENAKDLAYG AIVDIKDGTG RVRGGQVIEV SEEYAVIQVF
61: EETTGLDLAT TSVSLVEDVA RLGVSKEMLG RRFNGIGKPI DGLPPITPEK RLPITGLPLN
121: PVARRKPEQF IQTGISTIDV MNTLVRGQKL PIFSGSGLPA NEIAAQIARQ ATVRPDLSGE
181: GEKEEPFAVV FAAMGITQRE LSYFIQEFER TGALSRSVLF LNKADDPTIE RILTPRMALT
241: VAEYLAFEHD YHVLVILTDM TNYCEALREI GAAREEIPGR RGYPGYMYTD LATIYERAGV
301: VEGKKGSVTQ IPILSMPDDD RTHPIPDLTG YITEGQIQLS RELHRKGIYP PIDPLPSLSR
361: LMNNGVGKGK TREDHKQVSD QLYSAYANGV DIRKLVAIIG EDALTENDRR YLQFADAFER
421: FFINQGQQNR SIEESLQIAW ALLSMLPQGE LKRISKDHIG KYYGQKLEEI WGAPQALD