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Structural elements of the C-terminal domain of subunit E (E133-222) from the Saccharomyces cerevisiae V1VO ATPase determined by solution NMR spectroscopy

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Abstract

Subunit E of the vacuolar ATPase (V-ATPase) contains an N-terminal extended α helix (Rishikesan et al. J Bioenerg Biomembr 43:187–193, 2011) and a globular C-terminal part that is predicted to consist of a mixture of α-helices and β-sheets (Grüber et al. Biochem Biophys Res Comm 298:383–391, 2002). Here we describe the production, purification and 2D structure of the C-terminal segment E133-222 of subunit E from Saccharamyces cerevisiae V-ATPase in solution based on the secondary structure calculation from NMR spectroscopy studies. E133-222 consists of four β-strands, formed by the amino acids from K136-V139, E170-V173, G186-V189, D195-E198 and two α-helices, composed of the residues from R144-A164 and T202-I218. The sheets and helices are arranged as β1:α1:β2:β3:β4:α2, which are connected by flexible loop regions. These new structural details of subunit E are discussed in the light of the structural arrangements of this subunit inside the V1- and V1VO ATPase.

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Authors and Affiliations

  1. School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore, 637551, Republic of Singapore

    Sankaranarayanan Rishikesan & Gerhard Grüber

Authors
  1. Sankaranarayanan Rishikesan
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  2. Gerhard Grüber
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Corresponding author

Correspondence to Gerhard Grüber.

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Table S1

13C chemical shifts obtained from the solution NMR spectroscopy of E133-222 from S. cerevisiae V-ATPase. (DOC 115 kb)

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Rishikesan, S., Grüber, G. Structural elements of the C-terminal domain of subunit E (E133-222) from the Saccharomyces cerevisiae V1VO ATPase determined by solution NMR spectroscopy. J Bioenerg Biomembr 43, 447–455 (2011). https://doi.org/10.1007/s10863-011-9379-y

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  • DOI: https://doi.org/10.1007/s10863-011-9379-y

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