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PDBsum entry 5efw
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Signaling protein
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PDB id
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5efw
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PDB id:
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| Name: |
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Signaling protein
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Title:
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Crystal structure of lov2-zdk1 - the complex of oat lov2 and the affibody protein zdark1
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Structure:
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Nph1-1. Chain: a. Fragment: unp residues 404-546. Engineered: yes. Mutation: yes. Other_details: cys450ala mutation introduced to render the protein light inactive. Z-dark, a small protein based on the z domain affibody. Chain: b, c.
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Source:
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Avena sativa. Oat. Organism_taxid: 4498. Gene: nph1-1. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Staphylococcus aureus. Organism_taxid: 1280. Expressed in: escherichia coli.
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Resolution:
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2.10Å
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R-factor:
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0.205
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R-free:
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0.257
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Authors:
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A.Winkler,H.Wang,E.Hartmann,K.Hahn,I.Schlichting
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Key ref:
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H.Wang
et al.
(2016).
LOVTRAP: an optogenetic system for photoinduced protein dissociation.
Nat Methods,
13,
755-758.
PubMed id:
DOI:
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Date:
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10-Sep-14
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Release date:
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20-Jul-16
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PROCHECK
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Headers
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References
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O49003
(O49003_AVESA) -
non-specific serine/threonine protein kinase from Avena sativa
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Seq:
Struc:
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923 a.a.
141 a.a.*
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Enzyme class:
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Chain A:
E.C.2.7.11.1
- non-specific serine/threonine protein kinase.
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Reaction:
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1.
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L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H+
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2.
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L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H+
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L-seryl-[protein]
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+
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ATP
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=
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O-phospho-L-seryl-[protein]
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+
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ADP
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+
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H(+)
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L-threonyl-[protein]
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+
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ATP
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=
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O-phospho-L-threonyl-[protein]
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+
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ADP
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+
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H(+)
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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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Nat Methods
13:755-758
(2016)
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PubMed id:
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LOVTRAP: an optogenetic system for photoinduced protein dissociation.
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H.Wang,
M.Vilela,
A.Winkler,
M.Tarnawski,
I.Schlichting,
H.Yumerefendi,
B.Kuhlman,
R.Liu,
G.Danuser,
K.M.Hahn.
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ABSTRACT
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LOVTRAP is an optogenetic approach for reversible light-induced protein
dissociation using protein A fragments that bind to the LOV domain only in the
dark, with tunable kinetics and a >150-fold change in the dissociation
constant (Kd). By reversibly sequestering proteins at mitochondria, we precisely
modulated the proteins' access to the cell edge, demonstrating a naturally
occurring 3-mHz cell-edge oscillation driven by interactions of Vav2, Rac1, and
PI3K proteins.
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