cd18119

V/A-type ATP synthase catalytic subunit A (alpha), N-terminal domain

CDD entry
Member databaseCDD
CDD typedomain
Short nameATP-synt_V_A-type_alpha_N
SetATP-synt_F1_V1_A1_AB_FliI_N

Description

The alpha (A) subunit of the V1/A1 complexes of V/A-type ATP synthases, N-terminal domain. The V- and A-type family of ATPases are composed of two linked multi-subunit complexes: the V1 or A1 complex contain three copies each of the alpha and beta subunits that form the soluble catalytic core, which is involved in ATP synthesis/hydrolysis, and the Vo or Ao complex that forms the membrane-embedded proton pore. The A-ATP synthase (AoA1-ATPase) is found in archaea and functions like F-ATP synthase. Structurally, however, the A-ATP synthase is more closely related to the V-ATP synthase (vacuolar VoV1-ATPase), which is a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, the V- and A-type synthases can function in both ATP synthesis and hydrolysis modes.
[11, 9, 10, 14, 1, 12, 13, 7, 2, 8, 6, 16, 4, 3, 17, 15, 5]

References

1.Rotary protein motors. Oster G, Wang H. Trends Cell Biol 13, 114-21, (2003). PMID: 12628343

2.The molecular mechanism of ATP synthesis by F1F0-ATP synthase: a scrutiny of the major possibilities. Nath S. Adv. Biochem. Eng. Biotechnol. 74, 65-98, (2002). PMID: 11991184

3.New insights into structure-function relationships between archeal ATP synthase (A1A0) and vacuolar type ATPase (V1V0). Gruber G, Marshansky V. Bioessays 30, 1096-109, (2008). View articlePMID: 18937357

4.F-type or V-type? The chimeric nature of the archaebacterial ATP synthase. Schafer G, Meyering-Vos M. Biochim. Biophys. Acta 1101, 232-5, (1992). PMID: 1385979

5.The evolution of A-, F-, and V-type ATP synthases and ATPases: reversals in function and changes in the H+/ATP coupling ratio. Cross RL, Muller V. FEBS Lett. 576, 1-4, (2004). View articlePMID: 15473999

6.Crystal structure of the archaeal A1Ao ATP synthase subunit B from Methanosarcina mazei Go1: Implications of nucleotide-binding differences in the major A1Ao subunits A and B. Schafer IB, Bailer SM, Duser MG, Borsch M, Bernal RA, Stock D, Gruber G. J. Mol. Biol. 358, 725-40, (2006). View articlePMID: 16563431

7.The molecular mechanism of ATP synthesis by F1F0-ATP synthase. Senior AE, Nadanaciva S, Weber J. Biochim Biophys Acta 1553, 188-211, (2002). PMID: 11997128

8.Mechanism of the F(1)F(0)-type ATP synthase, a biological rotary motor. Capaldi RA, Aggeler R. Trends Biochem. Sci. 27, 154-60, (2002). View articlePMID: 11893513

9.The crystal structure of the nucleotide-free alpha 3 beta 3 subcomplex of F1-ATPase from the thermophilic Bacillus PS3 is a symmetric trimer. Shirakihara Y, Leslie AG, Abrahams JP, Walker JE, Ueda T, Sekimoto Y, Kambara M, Saika K, Kagawa Y, Yoshida M. Structure 5, 825-36, (1997). View articlePMID: 9261073

10.ATP synthesis driven by proton transport in F1F0-ATP synthase. Weber J, Senior AE. FEBS Lett. 545, 61-70, (2003). View articlePMID: 12788493

11.Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria. Abrahams JP, Leslie AG, Lutter R, Walker JE. Nature 370, 621-8, (1994). View articlePMID: 8065448

12.Structures and interactions of proteins involved in the coupling function of the protonmotive F(o)F(1)-ATP synthase. Gaballo A, Zanotti F, Papa S. Curr. Protein Pept. Sci. 3, 451-60, (2002). View articlePMID: 12370007

13.Coupling proton movements to c-ring rotation in F(1)F(o) ATP synthase: aqueous access channels and helix rotations at the a-c interface. Fillingame RH, Angevine CM, Dmitriev OY. Biochim Biophys Acta 1555, 29-36, (2002). PMID: 12206887

14.Understanding ATP synthesis: structure and mechanism of the F1-ATPase (Review). Leyva JA, Bianchet MA, Amzel LM. Mol. Membr. Biol. 20, 27-33, (2003). PMID: 12745923

15.Regulation and isoform function of the V-ATPases. Toei M, Saum R, Forgac M. Biochemistry 49, 4715-23, (2010). View articlePMID: 20450191

16.ATP synthases from archaea: the beauty of a molecular motor. Gruber G, Manimekalai MS, Mayer F, Muller V. Biochim Biophys Acta 1837, 940-52, (2014). PMID: 24650628

17.F-and V-ATPases in the genus Thermus and related species. Radax C, Sigurdsson O, Hreggvidsson GO, Aichinger N, Gruber C, Kristjansson JK, Stan-Lotter H. Syst. Appl. Microbiol. 21, 12-22, (1998). PMID: 9741106

External Links
This website requires cookies, and the limited processing of your personal data in order to function. By using the site you are agreeing to this as outlined in our Privacy Notice and Terms of Use.