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PDBsum entry 5d80
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Contents |
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(+ 0 more)
591 a.a.
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(+ 0 more)
457 a.a.
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445 a.a.
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104 a.a.
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216 a.a.
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203 a.a.
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88 a.a.
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81 a.a.
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178 a.a.
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68 a.a.
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223 a.a.
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212 a.a.
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115 a.a.
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PDB id:
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| Name: |
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Hydrolase
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Title:
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Crystal structure of yeast v1-atpase in the autoinhibited form
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Structure:
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V-type proton atpase catalytic subunit a. Chain: a, b, c, a, b, c. Synonym: v-atpase subunit a,vacuolar proton pump subunit a. V-type proton atpase subunit b. Chain: d, e, f, d, e, f. Synonym: v-atpase subunit b,v-atpase 57 kda subunit,vacuolar proton pump subunit b. V-type proton atpase subunit h. Chain: h, h.
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Source:
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Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 559292. Strain: atcc 204508 / s288c. Variant: vma5 delete. Variant: vma5 delete
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Resolution:
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6.20Å
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R-factor:
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0.257
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R-free:
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0.302
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Authors:
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R.A.Oot,P.M.Kane,E.A.Berry,S.Wilkens
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Key ref:
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R.A.Oot
et al.
(2016).
Crystal structure of yeast V1-ATPase in the autoinhibited state.
Embo J,
35,
1694-1706.
PubMed id:
DOI:
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Date:
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14-Aug-15
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Release date:
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08-Jun-16
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PROCHECK
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Headers
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References
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P17255
(VATA_YEAST) -
V-type proton ATPase catalytic subunit A from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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Seq:
Struc:
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1071 a.a.
591 a.a.
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P16140
(VATB_YEAST) -
V-type proton ATPase subunit B from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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Seq:
Struc:
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517 a.a.
457 a.a.
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P41807
(VATH_YEAST) -
V-type proton ATPase subunit H from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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Seq:
Struc:
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478 a.a.
445 a.a.
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P48836
(VATG_YEAST) -
V-type proton ATPase subunit G from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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Seq:
Struc:
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114 a.a.
104 a.a.
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P22203
(VATE_YEAST) -
V-type proton ATPase subunit E from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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Seq:
Struc:
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233 a.a.
216 a.a.
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P22203
(VATE_YEAST) -
V-type proton ATPase subunit E from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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Seq:
Struc:
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233 a.a.
203 a.a.
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P48836
(VATG_YEAST) -
V-type proton ATPase subunit G from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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Seq:
Struc:
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114 a.a.
88 a.a.
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P48836
(VATG_YEAST) -
V-type proton ATPase subunit G from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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Seq:
Struc:
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114 a.a.
81 a.a.
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P22203
(VATE_YEAST) -
V-type proton ATPase subunit E from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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Seq:
Struc:
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233 a.a.
178 a.a.
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P48836
(VATG_YEAST) -
V-type proton ATPase subunit G from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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Seq:
Struc:
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114 a.a.
68 a.a.
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P32610
(VATD_YEAST) -
V-type proton ATPase subunit D from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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Seq:
Struc:
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256 a.a.
223 a.a.
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Enzyme class 2:
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Chains A, B, C, a, b, c:
E.C.3.1.-.-
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Enzyme class 3:
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Chains A, B, C, a, b, c:
E.C.7.1.2.2
- H(+)-transporting two-sector ATPase.
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Reaction:
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ATP + H2O + 4 H+(in) = ADP + phosphate + 5 H+(out)
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ATP
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+
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H2O
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+
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4
×
H(+)(in)
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=
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ADP
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+
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phosphate
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+
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5
×
H(+)(out)
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Enzyme class 4:
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Chains D, E, F, H, J, I, K, L, M, N, d, e, f, h, j, i, k, l, m, n, G, g, o, O:
E.C.3.6.3.14
- Transferred entry: 7.1.2.2.
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Reaction:
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ATP + H2O + H+(In) = ADP + phosphate + H+(Out)
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ATP
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+
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H(2)O
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+
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4
×
H(+)(In)
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=
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ADP
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+
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phosphate
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+
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5
×
H(+)(Out)
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Note, where more than one E.C. class is given (as above), each may
correspond to a different protein domain or, in the case of polyprotein
precursors, to a different mature protein.
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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DOI no:
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Embo J
35:1694-1706
(2016)
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PubMed id:
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| |
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Crystal structure of yeast V1-ATPase in the autoinhibited state.
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R.A.Oot,
P.M.Kane,
E.A.Berry,
S.Wilkens.
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ABSTRACT
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Vacuolar ATPases (V-ATPases) are essential proton pumps that acidify the lumen
of subcellular organelles in all eukaryotic cells and the extracellular space in
some tissues. V-ATPase activity is regulated by a unique mechanism referred to
as reversible disassembly, wherein the soluble catalytic sector, V1, is released
from the membrane and its MgATPase activity silenced. The crystal structure of
yeast V1 presented here shows that activity silencing involves a large
conformational change of subunit H, with its C-terminal domain rotating ~150°
from a position near the membrane in holo V-ATPase to a position at the bottom
of V1 near an open catalytic site. Together with biochemical data, the structure
supports a mechanistic model wherein subunit H inhibits ATPase activity by
stabilizing an open catalytic site that results in tight binding of inhibitory
ADP at another site.
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