Solution structure of subunit F (Vma7p) of the eukaryotic V(1)V(O) ATPase from Saccharomyces cerevesiae derived from SAXS and NMR spectroscopy.
Biochim Biophys Acta. 2010 Sep 11;
Authors: Basak S, Gayen S, Thaker YR, Manimekalai MS, Roessle M, Hunke C, Grüber G
Vacuolar ATPases uses the energy derived from ATP hydrolysis, catalyzed in the A(3)B(3) sector of the V(1) ATPase to pump protons via the membrane-embedded V(O) sector. The energy coupling between the two sectors occurs via the so-called central stalk, to which subunit F does belong. Here we present the first low resolution structure of recombinant subunit F (Vma7p) of a eukaryotic V-ATPase from Saccharomyces cerevisiae, analyzed by small angle X-ray scattering (SAXS). The protein is divided into a 5.5nm long egg-like shaped region, connected via a 1.5nm linker to a hook-like segment at one end. Circular dichroism spectroscopy revealed that subunit F comprises of 43% α-helix, 32% β-sheet and a 25% random coil arrangement. To determine the localization of the N- and C-termini in the protein, the C-terminal truncated form of F, F(1-94) was produced and analyzed by SAXS. Comparison of the F(1-94) shape with the one of subunit F showed the missing hook-like region in F(1-94), supported by the decreased D(max) value of F(1-94) (7.0nm), and indicating that the hook-like region consists of the C-terminal residues. The NMR solution structure of the C-terminal peptide, F(90-116), was solved, displaying an α-helical region between residues 103-113. The F(90-116) solution structure fitted well in the hook-like region of subunit F. Finally, the arrangement of subunit F within the V(1) ATPase is discussed.
PMID: 20840841 [PubMed - as supplied by publisher]
Solution NMR structure of MED25(391-543) comprising the activator-interacting domain (ACID) of human mediator subunit 25.
Solution NMR structure of MED25(391-543) comprising the activator-interacting domain (ACID) of human mediator subunit 25.
Solution NMR structure of MED25(391-543) comprising the activator-interacting domain (ACID) of human mediator subunit 25.
J Struct Funct Genomics. 2011 Jul 23;
Authors: Eletsky A, Ruyechan WT, Xiao R, Acton TB, Montelione GT, Szyperski T
The solution NMR structure of protein MED25(391-543), comprising the activator interacting domain (ACID) of subunit 25 of the human mediator, is presented along with the measurement of...
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07-26-2011 09:30 PM
NMR solution structure of subunit E (fragment E(1-69)) of the Saccharomyces cerevisiae V (1)V (O) ATPase.
NMR solution structure of subunit E (fragment E(1-69)) of the Saccharomyces cerevisiae V (1)V (O) ATPase.
NMR solution structure of subunit E (fragment E(1-69)) of the Saccharomyces cerevisiae V (1)V (O) ATPase.
J Bioenerg Biomembr. 2011 Mar 12;
Authors: Rishikesan S, Thaker YR, Grüber G
The N-terminus of V-ATPase subunit E has been shown to associate with the subunits C, G and H, respectively. To understand the assembly of E with its neighboring subunits as well as its N-terminal structure, the N-terminal region, E(1-69), of the...
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03-15-2011 04:06 PM
[NMR paper] NMR solution structure of calerythrin, an EF-hand calcium-binding protein from Saccha
NMR solution structure of calerythrin, an EF-hand calcium-binding protein from Saccharopolyspora erythraea.
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Eur J Biochem. 2003 Jun;270(11):2505-12
Authors: Tossavainen H, Permi P, Annila A, Kilpeläinen I, Drakenberg T
The structure of calerythrin, a prokaryotic 20 kDa calcium-binding protein has been determined by solution NMR spectroscopy. Distance, dihedral angle, J coupling, secondary chemical shift, residual dipolar...
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11-24-2010 09:01 PM
[NMR paper] Activity and NMR structure of synthetic peptides of the bovine ATPase inhibitor prote
Activity and NMR structure of synthetic peptides of the bovine ATPase inhibitor protein, IF1.
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Peptides. 2002 Dec;23(12):2127-41
Authors: de Chiara C, Nicastro G, Spisni A, Zanotti F, Cocco T, Papa S
The protein IF(1) is a natural inhibitor of the mitochondrial F(o)F(1)-ATPase. Many investigators have been prompted to identify the shortest segment of IF(1), retaining its native activity, for use in biomedical applications. Here, the...
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11-24-2010 08:58 PM
[NMR paper] Solution NMR structure and backbone dynamics of the PsaE subunit of photosystem I fro
Solution NMR structure and backbone dynamics of the PsaE subunit of photosystem I from Synechocystis sp. PCC 6803.
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Biochemistry. 2002 Nov 26;41(47):13902-14
Authors: Barth P, Savarin P, Gilquin B, Lagoutte B, Ochsenbein F
PsaE is a small peripheral subunit of photosystem I (PSI) that is very accessible to the surrounding medium. It plays an essential role in optimizing the interactions with the soluble electron...
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11-24-2010 08:58 PM
[NMR paper] NMR structure of conserved eukaryotic protein ZK652.3 from C. elegans: a ubiquitin-li
NMR structure of conserved eukaryotic protein ZK652.3 from C. elegans: a ubiquitin-like fold.
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Proteins. 2002 Sep 1;48(4):733-6
Authors: Cort JR, Chiang Y, Zheng D, Montelione GT, Kennedy MA
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[NMR paper] NMR structure of the N-SH2 of the p85 subunit of phosphoinositide 3-kinase complexed
NMR structure of the N-SH2 of the p85 subunit of phosphoinositide 3-kinase complexed to a doubly phosphorylated peptide reveals a second phosphotyrosine binding site.
Related Articles NMR structure of the N-SH2 of the p85 subunit of phosphoinositide 3-kinase complexed to a doubly phosphorylated peptide reveals a second phosphotyrosine binding site.
Biochemistry. 2000 Dec 26;39(51):15860-9
Authors: Weber T, Schaffhausen B, Liu Y, Günther UL
The N-terminal src homology 2 (SH2) domain of the p85 subunit of phosphoinositide 3-kinase (PI3K) has a...
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[NMR paper] NMR solution structure of the theta subunit of DNA polymerase III from Escherichia co
NMR solution structure of the theta subunit of DNA polymerase III from Escherichia coli.
Related Articles NMR solution structure of the theta subunit of DNA polymerase III from Escherichia coli.
Protein Sci. 2000 Apr;9(4):721-33
Authors: Keniry MA, Berthon HA, Yang JY, Miles CS, Dixon NE
The catalytic core of Escherichia coli DNA polymerase III contains three tightly associated subunits (alpha, epsilon, and theta). The theta subunit is the smallest, but the least understood of the three. As a first step in a program aimed at understanding its...