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PDBsum entry 1bvh
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Hydrolase PDB id
1bvh

 

 

 

 

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Contents
Protein chain
157 a.a. *
* Residue conservation analysis
PDB id:
1bvh
Name: Hydrolase
Title: Solution structure of a low molecular weight protein tyrosine phosphatase
Structure: Acid phosphatase. Chain: a. Engineered: yes
Source: Bos taurus. Cattle. Organism_taxid: 9913. Organ: heart. Expressed in: escherichia coli. Expression_system_taxid: 562
NMR struc: 15 models
Authors: T.M.Logan,M.-M.Zhou,D.G.Nettesheim,R.P.Meadows,R.L.Van Etten, S.W.Fesik
Key ref:
T.M.Logan et al. (1994). Solution structure of a low molecular weight protein tyrosine phosphatase. Biochemistry, 33, 11087-11096. PubMed id: 7727361 DOI: 10.1021/bi00203a005
Date:
03-May-94     Release date:   31-Jul-94    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P11064  (PPAC_BOVIN) -  Low molecular weight phosphotyrosine protein phosphatase from Bos taurus
Seq:
Struc: 		158 a.a.
157 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class 2: E.C.3.1.3.2  - acid phosphatase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: a phosphate monoester + H2O = an alcohol + phosphate
phosphate monoester
 + H2O
 = alcohol
 + phosphate
   Enzyme class 3: E.C.3.1.3.48  - protein-tyrosine-phosphatase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: O-phospho-L-tyrosyl-[protein] + H2O = L-tyrosyl-[protein] + phosphate
O-phospho-L-tyrosyl-[protein]
 + H2O
 = L-tyrosyl-[protein]
 + phosphate
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.
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
DOI no: 10.1021/bi00203a005 Biochemistry 33:11087-11096 (1994)
PubMed id: 7727361  
 
 
Solution structure of a low molecular weight protein tyrosine phosphatase.
T.M.Logan, M.M.Zhou, D.G.Nettesheim, R.P.Meadows, R.L.Van Etten, S.W.Fesik.
 
  ABSTRACT  
 
Protein tyrosine phosphatases (PTPs) are important enzymes involved in signal transduction, cell cycle regulation, and the control of differentiation. Despite the importance of this class of enzymes in the control of critical cell processes, very little structural information is available for this family of proteins. In this paper, we present the first solution structure of a protein tyrosine phosphatase. This protein is a low molecular weight cytosolic PTP that was initially isolated from bovine heart. The structure that was determined from 1747 NMR-derived restraints consists of a central four-stranded parallel beta-sheet surrounded by four alpha-helices and a short 3(10) helix. The phosphate binding site, identified by chemical shift changes upon the addition of the competitive inhibitors phosphate and vanadate, is in a loop region connecting the C-terminal end of the first beta-strand with the first alpha-helix. Residues in the second, fourth, and fifth alpha-helices and in some of the loop regions connecting the elements of regular secondary structure also contribute to the binding site. The structure determined here is consistent with previous mutagenesis and chemical modification studies conducted on this protein.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
18004775 L.Cunha, M.Kuti, D.F.Bishop, M.Mezei, L.Zeng, M.M.Zhou, and R.J.Desnick (2008).
Human uroporphyrinogen III synthase: NMR-based mapping of the active site.
  Proteins, 71, 855-873.  
17008719 D.Tolkatchev, R.Shaykhutdinov, P.Xu, J.Plamondon, D.C.Watson, N.M.Young, and F.Ni (2006).
Three-dimensional structure and ligand interactions of the low molecular weight protein tyrosine phosphatase from Campylobacter jejuni.
  Protein Sci, 15, 2381-2394.
PDB code: 2gi4
16651264 E.Lescop, Y.Hu, H.Xu, W.Hu, J.Chen, B.Xia, and C.Jin (2006).
The solution structure of Escherichia coli Wzb reveals a novel substrate recognition mechanism of prokaryotic low molecular weight protein-tyrosine phosphatases.
  J Biol Chem, 281, 19570-19577.
PDB code: 2fek
16452434 H.Xu, B.Xia, and C.Jin (2006).
Solution structure of a low-molecular-weight protein tyrosine phosphatase from Bacillus subtilis.
  J Bacteriol, 188, 1509-1517.
PDB code: 1zgg
16195543 C.L.Gustafson, C.V.Stauffacher, K.Hallenga, and R.L.Van Etten (2005).
Solution structure of the low-molecular-weight protein tyrosine phosphatase from Tritrichomonas foetus reveals a flexible phosphate binding loop.
  Protein Sci, 14, 2515-2525.
PDB code: 1p8a
15258141 P.M.Legler, M.Cai, A.Peterkofsky, and G.M.Clore (2004).
Three-dimensional solution structure of the cytoplasmic B domain of the mannitol transporter IImannitol of the Escherichia coli phosphotransferase system.
  J Biol Chem, 279, 39115-39121.
PDB code: 1vkr
12682056 N.Lah, J.Lah, I.Zegers, L.Wyns, and J.Messens (2003).
Specific potassium binding stabilizes pI258 arsenate reductase from Staphylococcus aureus.
  J Biol Chem, 278, 24673-24679.  
11573087 I.Zegers, J.C.Martins, R.Willem, L.Wyns, and J.Messens (2001).
Arsenate reductase from S. aureus plasmid pI258 is a phosphatase drafted for redox duty.
  Nat Struct Biol, 8, 843-847.
PDB codes: 1jf8 1jfv
10684639 S.Wang, L.Tabernero, M.Zhang, E.Harms, R.L.Van Etten, and C.V.Stauffacher (2000).
Crystal structures of a low-molecular weight protein tyrosine phosphatase from Saccharomyces cerevisiae and its complex with the substrate p-nitrophenyl phosphate.
  Biochemistry, 39, 1903-1914.
PDB codes: 1d1p 1d1q
10409830 K.Kolmodin, P.Nordlund, and J.Aqvist (1999).
Mechanism of substrate dephosphorylation in low Mr protein tyrosine phosphatase.
  Proteins, 36, 370-379.  
10052933 M.Zhou, and R.L.Van Etten (1999).
Structural basis of the tight binding of pyridoxal 5'-phosphate to a low molecular weight protein tyrosine phosphatase.
  Biochemistry, 38, 2636-2646.  
9705307 M.Zhang, C.V.Stauffacher, D.Lin, and R.L.Van Etten (1998).
Crystal structure of a human low molecular weight phosphotyrosyl phosphatase. Implications for substrate specificity.
  J Biol Chem, 273, 21714-21720.
PDB code: 5pnt
9147129 G.Ramponi, and M.Stefani (1997).
Structural, catalytic, and functional properties of low M(r), phosphotyrosine protein phosphatases. Evidence of a long evolutionary history.
  Int J Biochem Cell Biol, 29, 279-292.  
9295292 M.J.Pregel, and A.C.Storer (1997).
Active site titration of the tyrosine phosphatases SHP-1 and PTP1B using aromatic disulfides. Reaction with the essential cysteine residue in the active site.
  J Biol Chem, 272, 23552-23558.  
8993313 M.Zhang, M.Zhou, R.L.Van Etten, and C.V.Stauffacher (1997).
Crystal structure of bovine low molecular weight phosphotyrosyl phosphatase complexed with the transition state analog vanadate.
  Biochemistry, 36, 15-23.
PDB codes: 1dg9 1z12 1z13
9305993 P.A.Tishmack, D.Bashford, E.Harms, and R.L.Van Etten (1997).
Use of 1H NMR spectroscopy and computer simulations To analyze histidine pKa changes in a protein tyrosine phosphatase: experimental and theoretical determination of electrostatic properties in a small protein.
  Biochemistry, 36, 11984-11994.  
8885840 B.Evans, P.A.Tishmack, C.Pokalsky, M.Zhang, and R.L.Van Etten (1996).
Site-directed mutagenesis, kinetic, and spectroscopic studies of the P-loop residues in a low molecular weight protein tyrosine phosphatase.
  Biochemistry, 35, 13609-13617.  
  8771191 J.W.Eckstein, P.Beer-Romero, and I.Berdo (1996).
Identification of an essential acidic residue in Cdc25 protein phosphatase and a general three-dimensional model for a core region in protein phosphatases.
  Protein Sci, 5, 5.  
8617791 X.Xu, and S.P.Burke (1996).
Roles of active site residues and the NH2-terminal domain in the catalysis and substrate binding of human Cdc25.
  J Biol Chem, 271, 5118-5124.  
7876123 C.Pokalsky, P.Wick, E.Harms, F.E.Lytle, and R.L.Van Etten (1995).
Fluorescence resolution of the intrinsic tryptophan residues of bovine protein tyrosyl phosphatase.
  J Biol Chem, 270, 3809-3815.  
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.

 

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