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PDBsum entry 2m10
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PDB id:
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Hydrolase
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Title:
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Trans form of a photoswitchable pdz domain crosslinked with an azobenzene derivative
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Structure:
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Tyrosine-protein phosphatase non-receptor type 13. Chain: a. Fragment: pdz 2 domain residues 1361-1456. Synonym: fas-associated protein-tyrosine phosphatase 1, fap-1, ptp- bas, protein-tyrosine phosphatase 1e, ptp-e1, hptpe1, protein- tyrosine phosphatase ptpl1. Engineered: yes. Mutation: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: ptpn13, pnp1, ptp1e, ptpl1. Expressed in: escherichia coli. Expression_system_taxid: 469008.
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NMR struc:
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20 models
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Authors:
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R.Walser
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Key ref:
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B.Buchli
et al.
(2013).
Kinetic response of a photoperturbed allosteric protein.
Proc Natl Acad Sci U S A,
110,
11725-11730.
PubMed id:
DOI:
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Date:
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09-Nov-12
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Release date:
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03-Jul-13
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PROCHECK
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Headers
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References
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Q12923
(PTN13_HUMAN) -
Tyrosine-protein phosphatase non-receptor type 13 from Homo sapiens
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Seq:
Struc:
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2485 a.a.
97 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 3 residue positions (black
crosses)
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Enzyme class:
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E.C.3.1.3.48
- protein-tyrosine-phosphatase.
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Reaction:
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O-phospho-L-tyrosyl-[protein] + H2O = L-tyrosyl-[protein] + phosphate
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O-phospho-L-tyrosyl-[protein]
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+
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H2O
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=
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L-tyrosyl-[protein]
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+
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phosphate
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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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Proc Natl Acad Sci U S A
110:11725-11730
(2013)
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PubMed id:
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Kinetic response of a photoperturbed allosteric protein.
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B.Buchli,
S.A.Waldauer,
R.Walser,
M.L.Donten,
R.Pfister,
N.Blöchliger,
S.Steiner,
A.Caflisch,
O.Zerbe,
P.Hamm.
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ABSTRACT
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By covalently linking an azobenzene photoswitch across the binding groove of a
PDZ domain, a conformational transition, similar to the one occurring upon
ligand binding to the unmodified domain, can be initiated on a picosecond
timescale by a laser pulse. The protein structures have been characterized in
the two photoswitch states through NMR spectroscopy and the transition between
them through ultrafast IR spectroscopy and molecular dynamics simulations. The
binding groove opens on a 100-ns timescale in a highly nonexponential manner,
and the molecular dynamics simulations suggest that the process is governed by
the rearrangement of the water network on the protein surface. We propose this
rearrangement of the water network to be another possible mechanism of allostery.
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Links
