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PDBsum entry 1x24

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protein Protein-protein interface(s) links
Hydrolase PDB id
1x24
Jmol
Contents
Protein chains
152 a.a. *
* Residue conservation analysis
PDB id:
1x24
Name: Hydrolase
Title: Prl-1 (ptp4a)
Structure: Protein tyrosine phosphatase 4a1. Chain: a, b. Fragment: residues 1-160. Synonym: prl-1, ptp4a1. Engineered: yes
Source: Rattus norvegicus. Norway rat. Organism_taxid: 10116. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.
Biol. unit: Monomer (from PQS)
Resolution:
3.20Å     R-factor:   0.241     R-free:   0.285
Authors: Z.Y.Zhang,J.P.Sun,S.Liu,W.Q.Wang,H.Yang
Key ref:
J.P.Sun et al. (2005). Structure and biochemical properties of PRL-1, a phosphatase implicated in cell growth, differentiation, and tumor invasion. Biochemistry, 44, 12009-12021. PubMed id: 16142898 DOI: 10.1021/bi0509191
Date:
20-Apr-05     Release date:   11-Oct-05    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q78EG7  (TP4A1_RAT) -  Protein tyrosine phosphatase type IVA 1
Seq:
Struc:
173 a.a.
152 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.1.3.48  - Protein-tyrosine-phosphatase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Protein tyrosine phosphate + H2O = protein tyrosine + phosphate
Protein tyrosine phosphate
+ H(2)O
= protein tyrosine
+ phosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     membrane   9 terms 
  Biological process     peptidyl-tyrosine dephosphorylation   5 terms 
  Biochemical function     hydrolase activity     5 terms  

 

 
    reference    
 
 
DOI no: 10.1021/bi0509191 Biochemistry 44:12009-12021 (2005)
PubMed id: 16142898  
 
 
Structure and biochemical properties of PRL-1, a phosphatase implicated in cell growth, differentiation, and tumor invasion.
J.P.Sun, W.Q.Wang, H.Yang, S.Liu, F.Liang, A.A.Fedorov, S.C.Almo, Z.Y.Zhang.
 
  ABSTRACT  
 
The PRL (phosphatase of regenerating liver) phosphatases constitute a novel class of small, prenylated phosphatases that are implicated in promoting cell growth, differentiation, and tumor invasion, and represent attractive targets for anticancer therapy. Here we describe the crystal structures of native PRL-1 as well as the catalytically inactive mutant PRL-1/C104S in complex with sulfate. PRL-1 exists as a trimer in the crystalline state, burying 1140 A2 of accessible surface area at each dimer interface. Trimerization creates a large, bipartite membrane-binding surface in which the exposed C-terminal basic residues could cooperate with the adjacent prenylation group to anchor PRL-1 on the acidic inner membrane. Structural and kinetic analyses place PRL-1 in the family of dual specificity phopsphatases with closest structural similarity to the Cdc14 phosphatase and provide a molecular basis for catalytic activation of the PRL phosphatases. Finally, native PRL-1 is crystallized in an oxidized form in which a disulfide is formed between the active site Cys104 and a neighboring residue Cys49, which blocks both substrate binding and catalysis. Biochemical studies in solution and in the cell support a potential regulatory role of this intramolecular disulfide bond formation in response to reactive oxygen species such as H2O2.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
  21547913 K.W.Nti-Addae, J.S.Laurence, A.L.Skinner, and V.J.Stella (2011).
Reversion of sulfenamide prodrugs in the presence of free thiol-containing proteins.
  J Pharm Sci, 100, 3023-3027.  
21053359 A.Q.Al-Aidaroos, and Q.Zeng (2010).
PRL-3 phosphatase and cancer metastasis.
  J Cell Biochem, 111, 1087-1098.  
20679247 C.W.Vander Kooi, A.O.Taylor, R.M.Pace, D.A.Meekins, H.F.Guo, Y.Kim, and M.S.Gentry (2010).
Structural basis for the glucan phosphatase activity of Starch Excess4.
  Proc Natl Acad Sci U S A, 107, 15379-15384.
PDB code: 3nme
19634988 M.A.Wouters, S.W.Fan, and N.L.Haworth (2010).
Disulfides as redox switches: from molecular mechanisms to functional significance.
  Antioxid Redox Signal, 12, 53-91.  
19341304 A.L.Skinner, A.A.Vartia, T.D.Williams, and J.S.Laurence (2009).
Enzyme activity of phosphatase of regenerating liver is controlled by the redox environment and its C-terminal residues.
  Biochemistry, 48, 4262-4272.  
19636948 A.L.Skinner, and J.S.Laurence (2009).
1H, 15N, 13C resonance assignments of the reduced and active form of human Protein Tyrosine Phosphatase, PRL-1.
  Biomol NMR Assign, 3, 61-65.  
19415758 D.G.Jeong, S.K.Jung, T.S.Yoon, E.J.Woo, J.H.Kim, B.C.Park, S.E.Ryu, and S.J.Kim (2009).
Crystal structure of the catalytic domain of human MKP-2 reveals a 24-mer assembly.
  Proteins, 76, 763-767.
PDB code: 3ezz
19639556 L.Orsatti, F.Innocenti, P.Lo Surdo, F.Talamo, and G.Barbato (2009).
Mass spectrometry study of PRL-3 phosphatase inactivation by disulfide bond formation and cysteine into glycine conversion.
  Rapid Commun Mass Spectrom, 23, 2733-2740.  
19371084 S.J.Tsai, U.Sen, L.Zhao, W.B.Greenleaf, J.Dasgupta, E.Fiorillo, V.Orrú, N.Bottini, and X.S.Chen (2009).
Crystal structure of the human lymphoid tyrosine phosphatase catalytic domain: insights into redox regulation .
  Biochemistry, 48, 4838-4845.
PDB code: 3h2x
19598234 S.W.Fan, R.A.George, N.L.Haworth, L.L.Feng, J.Y.Liu, and M.A.Wouters (2009).
Conformational changes in redox pairs of protein structures.
  Protein Sci, 18, 1745-1765.  
19236507 X.Xing, L.Peng, L.Qu, T.Ren, B.Dong, X.Su, and C.Shou (2009).
Prognostic value of PRL-3 overexpression in early stages of colonic cancer.
  Histopathology, 54, 309-318.  
18224294 D.C.Bessette, D.Qiu, and C.J.Pallen (2008).
PRL PTPs: mediators and markers of cancer progression.
  Cancer Metastasis Rev, 27, 231-252.  
18433060 D.J.Aceti, E.Bitto, A.F.Yakunin, M.Proudfoot, C.A.Bingman, R.O.Frederick, H.K.Sreenath, F.C.Vojtik, R.L.Wrobel, B.G.Fox, J.L.Markley, and G.N.Phillips (2008).
Structural and functional characterization of a novel phosphatase from the Arabidopsis thaliana gene locus At1g05000.
  Proteins, 73, 241-253.
PDB code: 1xri
18259840 Z.X.Jiang, and Z.Y.Zhang (2008).
Targeting PTPs with small molecule inhibitors in cancer treatment.
  Cancer Metastasis Rev, 27, 263-272.  
17656357 J.P.Sun, Y.Luo, X.Yu, W.Q.Wang, B.Zhou, F.Liang, and Z.Y.Zhang (2007).
Phosphatase activity, trimerization, and the C-terminal polybasic region are all required for PRL1-mediated cell growth and migration.
  J Biol Chem, 282, 29043-29051.  
17505108 J.Phan, J.E.Tropea, and D.S.Waugh (2007).
Structure-assisted discovery of Variola major H1 phosphatase inhibitors.
  Acta Crystallogr D Biol Crystallogr, 63, 698-704.
PDB code: 2p4d
17673310 L.Yu, U.Kelly, J.N.Ebright, G.Malek, P.Saloupis, D.W.Rickman, B.S.McKay, V.Y.Arshavsky, and C.Bowes Rickman (2007).
Oxidative stress-induced expression and modulation of Phosphatase of Regenerating Liver-1 (PRL-1) in mammalian retina.
  Biochim Biophys Acta, 1773, 1473-1482.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.