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PDBsum entry 4hjp
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PDB id:
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Hydrolase
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Title:
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Shp-1 catalytic domain wpd loop open
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Structure:
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Tyrosine-protein phosphatase non-receptor type 6. Chain: a. Fragment: phosphatase domain (unp residues 242-528). Synonym: hematopoietic cell protein-tyrosine phosphatase, protein- tyrosine phosphatase 1c, ptp-1c, protein-tyrosine phosphatase shp-1, sh-ptp1. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: hcp, ptp1c, ptpn6, shp-1 (ptpn6). Expressed in: escherichia coli. Expression_system_taxid: 469008.
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Resolution:
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1.40Å
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R-factor:
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0.165
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R-free:
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0.186
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Authors:
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N.L.Alicea-Velazquez,T.J.Boggon
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Key ref:
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N.L.Alicea-Velazquez
and
T.J.Boggon
(2013).
SHP family protein tyrosine phosphatases adopt canonical active-site conformations in the apo and phosphate-bound states.
Protein Pept Lett,
20,
1039-1048.
PubMed id:
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Date:
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13-Oct-12
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Release date:
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03-Apr-13
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PROCHECK
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Headers
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References
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P29350
(PTN6_HUMAN) -
Tyrosine-protein phosphatase non-receptor type 6 from Homo sapiens
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Seq:
Struc:
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595 a.a.
281 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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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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Protein Pept Lett
20:1039-1048
(2013)
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PubMed id:
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SHP family protein tyrosine phosphatases adopt canonical active-site conformations in the apo and phosphate-bound states.
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N.L.Alicea-Velazquez,
T.J.Boggon.
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ABSTRACT
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Protein tyrosine phosphatase (PTP) catalytic domains undergo a series of
conformational changes in order to mediate dephosphorylation of their tyrosine
phosphorylated substrates. An important conformational change occurs in the
Tryptophan-Proline-Aspartic acid (WPD) loop, which contains the conserved
catalytic aspartate. Upon substrate binding, the WPD loop transitions from the
'open' to the 'closed' state, thus allowing optimal positioning of the catalytic
aspartate for substrate dephosphorylation. The dynamics of WPD loop
conformational changes have previously been studied for PTP1B, HePTP, and the
bacterial phosphatase YopH, but have not yet been comprehensively studied for
the nonreceptor tyrosine phosphatase SHP-1 (PTPN6). To structurally describe the
changes in WPD loop conformation in SHP-1, we have determined the 1.4 Å crystal
structure of the catalytic domain of SHP-1 in the Apo state and the 1.8 Å
crystal structure of the SHP-1 catalytic domain in complex with a phosphate ion.
We provide structural analysis for the WPD loop closed state of SHP phosphatases
and the conformational changes that occur upon WPD loop closure.
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