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PDBsum entry 4phh
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Endocytosis,exocytosis
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PDB id
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4phh
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PDB id:
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| Name: |
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Endocytosis,exocytosis
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Title:
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Crystal structure of ypt7 covalently modified with gnp
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Structure:
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Gtp-binding protein ypt7. Chain: a, b, c, d. Fragment: unp residues 1-182. Engineered: yes. Mutation: yes
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Source:
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Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 559292. Strain: s288c. Gene: ypt7, vam4, yml001w, ym8270.02. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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2.35Å
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R-factor:
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0.203
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R-free:
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0.263
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Authors:
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D.Wiegandt,S.Vieweg,F.Hofmann,D.Koch,Y.Wu,A.Itzen,M.P.Mueller, R.S.Goody
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Key ref:
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D.Wiegandt
et al.
(2015).
Locking GTPases covalently in their functional states.
Nat Commun,
6,
7773.
PubMed id:
DOI:
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Date:
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06-May-14
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Release date:
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28-May-14
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PROCHECK
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Headers
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References
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P32939
(YPT7_YEAST) -
Ypt/Rab-type GTPase YPT7 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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Seq:
Struc:
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208 a.a.
172 a.a.*
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Key: |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
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DOI no:
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Nat Commun
6:7773
(2015)
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PubMed id:
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Locking GTPases covalently in their functional states.
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D.Wiegandt,
S.Vieweg,
F.Hofmann,
D.Koch,
F.Li,
Y.W.Wu,
A.Itzen,
M.P.Müller,
R.S.Goody.
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ABSTRACT
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GTPases act as key regulators of many cellular processes by switching between
active (GTP-bound) and inactive (GDP-bound) states. In many cases, understanding
their mode of action has been aided by artificially stabilizing one of these
states either by designing mutant proteins or by complexation with
non-hydrolysable GTP analogues. Because of inherent disadvantages in these
approaches, we have developed acryl-bearing GTP and GDP derivatives that can be
covalently linked with strategically placed cysteines within the GTPase of
interest. Binding studies with GTPase-interacting proteins and X-ray
crystallography analysis demonstrate that the molecular properties of the
covalent GTPase-acryl-nucleotide adducts are a faithful reflection of those of
the corresponding native states and are advantageously permanently locked in a
defined nucleotide (that is active or inactive) state. In a first application,
in vivo experiments using covalently locked Rab5 variants provide new insights
into the mechanism of correct intracellular localization of Rab proteins.
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