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Open Access Green as soon as Postprint is submitted to ZB.
Structural analysis of the stalk subunit Vma5p of the yeast V-ATPase in solution.
FEBS Lett. 570, 119-25 (2004)
Vma5p (subunit C) of the yeast V-ATPase was produced in Escherichia coli and purified to homogeneity. Analysis of secondary structure by circular dichroism spectroscopy showed that Vma5p comprises 64% alpha-helix and 17% beta-sheet content. The molecular mass of this subunit, determined by gel filtration analysis and small angle X-ray scattering (SAXS), was approximately 51+/-4 kDa, indicating a high hydration level of the protein in solution. The radius of gyration and the maximum size of Vma5p were determined to be 3.74+/-0.03 and 12.5+/-0.1 nm, respectively. Using two independent ab initio approaches, the first low-resolution shape of the protein was determined. Vma5p is an elongated boot-shaped particle consisting of two distinct domains. Co-reconstitution of Vma5p to V1 without C from Manduca sexta resulted in a V1-Vma5p hybrid complex and a 20% increase in ATPase hydrolysis activity.
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Publication type
Article: Journal article
Document type
Scientific Article
Language
english
Publication Year
2004
HGF-reported in Year
0
ISSN (print) / ISBN
0014-5793
e-ISSN
1873-3468
Journal
FEBS Letters
Quellenangaben
Volume: 570,
Issue: 1-3,
Pages: 119-25
Publisher
Elsevier
Reviewing status
Peer reviewed
Institute(s)
Institute of Pancreatic Islet Research (IPI)
PubMed ID
15251451
Erfassungsdatum
2004-12-31