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Contents |
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* Residue conservation analysis
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PDB id:
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Hydrolase
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Title:
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Crystal structure of human mkp-2
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Structure:
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Dual specificity protein phosphatase 4. Chain: a, b, c, d, e, f. Fragment: catalytic domain. Synonym: mitogen-activated protein kinase phosphatase 2, map kinase phosphatase 2, mkp-2, dual specificity protein phosphatase hvh2. Engineered: yes. Mutation: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: dusp4, mkp2, vh2. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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2.90Å
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R-factor:
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0.219
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R-free:
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0.242
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Authors:
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D.G.Jeong,S.K.Jung,S.E.Ryu,S.J.Kim
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Key ref:
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D.G.Jeong
et al.
(2009).
Crystal structure of the catalytic domain of human MKP-2 reveals a 24-mer assembly.
Proteins,
76,
763-767.
PubMed id:
DOI:
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Date:
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24-Oct-08
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Release date:
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25-Aug-09
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PROCHECK
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Headers
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References
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Q13115
(DUS4_HUMAN) -
Dual specificity protein phosphatase 4
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Seq:
Struc:
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394 a.a.
144 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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*
PDB and UniProt seqs differ
at 2 residue positions (black
crosses)
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Enzyme class 1:
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E.C.3.1.3.16
- Phosphoprotein phosphatase.
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Reaction:
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A phosphoprotein + H2O = a protein + phosphate
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phosphoprotein
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+
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H(2)O
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=
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protein
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+
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phosphate
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Enzyme class 2:
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E.C.3.1.3.48
- Protein-tyrosine-phosphatase.
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Reaction:
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Protein tyrosine phosphate + H2O = protein tyrosine + phosphate
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Protein tyrosine phosphate
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+
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H(2)O
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=
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protein tyrosine
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+
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phosphate
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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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Gene Ontology (GO) functional annotation
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Biological process
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dephosphorylation
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2 terms
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Biochemical function
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phosphatase activity
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3 terms
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DOI no:
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Proteins
76:763-767
(2009)
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PubMed id:
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Crystal structure of the catalytic domain of human MKP-2 reveals a 24-mer assembly.
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D.G.Jeong,
S.K.Jung,
T.S.Yoon,
E.J.Woo,
J.H.Kim,
B.C.Park,
S.E.Ryu,
S.J.Kim.
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ABSTRACT
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Selected figure(s)
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Figure 1.
Figure 1. (a) A ribbon diagram of the Cys^280-Ser mutant of the
MKP-2C protomer. Secondary structural elements are labeled. The
bound sulfate ion indicates the position of the phosphate moiety
of the substrate, (b) C  trace
of MKP-2C is superimposed with that of VHR21 (pdb code: 1VHR).
GA: general acid residue (Asp 249 in MKP-2C), (c) Ribbon diagram
of 24-mer MKP-2C viewed along the pseudo-octahedral axis of
symmetry. Each protomer belonging to an individual tetrameric
unit is represented in the same color (cyan, yellow, green,
blue, orange and magenta). Fourfold NCS axes and the positions
of catalytic C280S are indicated, (d) Surface model of MKP-2C.
The surfaces of the MKP-2C 24-mer are shown. The point of view
and the color scheme are the same as in Figure 1(c). A tetramer
located at the top is omitted to allow a clear view of the
hollow space in the interior region, and (e) A stereo diagram of
the superimposed crystal structures of MKP-2C (pdb code: 3EZZ;
black), MKP-5C (pdb code: 1ZZW; green) and MKP-3C (pdb code:
1MKP; red). The structures were superimposed using the program
O.[18] The catalytic C280S is indicated as a black sphere.
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The above figure is
reprinted
by permission from John Wiley & Sons, Inc.:
Proteins
(2009,
76,
763-767)
copyright 2009.
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Links
