PDBsum entry 2i6j

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Hydrolase PDB id
Protein chain
161 a.a. *
Waters ×142
* Residue conservation analysis
PDB id:
Name: Hydrolase
Title: Crystal structure of the complex of the archaeal sulfolobus ptp-fold phosphatase with phosphate ion
Structure: Sulfolobus solfataricus protein tyrosine phosphatase. Chain: a. Synonym: ssoptp. Engineered: yes
Source: Sulfolobus solfataricus. Organism_taxid: 2287. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.
1.66Å     R-factor:   0.208     R-free:   0.241
Authors: H.M.Chu,A.H.J.Wang
Key ref:
H.M.Chu and A.H.Wang (2007). Enzyme-substrate interactions revealed by the crystal structures of the archaeal Sulfolobus PTP-fold phosphatase and its phosphopeptide complexes. Proteins, 66, 996. PubMed id: 17173287 DOI: 10.1002/prot.21262
29-Aug-06     Release date:   13-Mar-07    
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Protein chain
Pfam   ArchSchema ?
Q97VZ7  (Q97VZ7_SULSO) -  Uncharacterized protein
161 a.a.
161 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     peptidyl-tyrosine dephosphorylation   3 terms 
  Biochemical function     phosphatase activity     2 terms  


DOI no: 10.1002/prot.21262 Proteins 66:996 (2007)
PubMed id: 17173287  
Enzyme-substrate interactions revealed by the crystal structures of the archaeal Sulfolobus PTP-fold phosphatase and its phosphopeptide complexes.
H.M.Chu, A.H.Wang.
The P-loop-containing protein phos-phatases are important regulators in signal transduction. These enzymes have structural and functional similarity with a conserved sequence of Dx(25-41)HCxxGxxR(T/S) essential for catalysis. The singular protein tyrosine phosphatase (PTP) from archaeal Sulfolobus solfataricus is one of the smallest known PTPs with extreme thermostability. Here, we report the crystal structure of this phosphatase and its complexes with two tyrosyl phosphopeptides A-(p)Y-R and N-K-(p)Y-G-N. The structure suggests the minimal structural motif of the PTP family, having two variable sequences inserted between the beta2-beta3 and beta3-beta4 strands, respectively. The phosphate of both phosphopeptide substrates is bound to the P-loop through several hydrogen bonds. Comparison of several phosphatase-substrate complexes revealed that Gln135 on the Q-loop has different modes of recognition toward phosphopeptides. The substrate specificity of SsoPTP is primarily localized at the phosphotyrosine, suggesting that this phosphatase may be a prototypical PTP.
  Selected figure(s)  
Figure 1.
Figure 1. Structures of the SsoPTP in complex with phosphopeptides. (A) The view showing the overall structure of the SsoPTP-phosphopeptide (N-K-(p)Y-G-N) complex. The P-loop, D-loop, and Q-loop are in red, yellow, and green, respectively. The phosphopeptide substrate is shown as yellow color, and the density is 2F[o] - F[c] map contoured at 1.0 . (B) A GRASP electrostatic surface representation of the complex of the SsoPTP with phosphopeptide (A-(p)Y-R) potentials ranging from -15 eV (red) to +15 eV (blue). (C) Details of the interactions between phosphopeptide (N-K-(p)Y-G-N), PEG, metal ion and the SsoPTP. (D) An enlarged figure of surface potential shows the active site of the SsoPTP-N-K-(p)Y-G-N complex. (E) and (F) Schematic diagrams of interactions involved in A-(p)Y-R and N-K-(p)Y-G-N binding with SsoPTP.
Figure 3.
Figure 3. Comparison of the topology diagram of DSP fold phosphatases. (A) The topology of the SsoPTP. (B) The structural features of P-loop containing phosphatases divided into a most conserved region and two diverse loop regions (Box1 and Box2). (C) Ribbon and surface diagrams of SsoPTP reveal the region of Box1 and Box2, which is associated with the major diversity in many PTPs and DSPs.
  The above figures are reprinted by permission from John Wiley & Sons, Inc.: Proteins (2007, 66, 996-0) copyright 2007.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
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
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