2DXP

Crystal structure of the complex of the archaeal sulfolobus PTP-fold phosphatase with phosphopeptides A-(p)Y-R

Summary for 2DXP

• Entry DOI: 10.2210/pdb2dxp/pdb
• Related: 2I6I 2I6J 2I6M 2I6O 2I6P
• Descriptor: Sulfolobus solfataricus protein tyrosine phosphatase, A(PTR)R (3 entities in total)
• Functional Keywords: ptp domain, hydrolase
• Biological source: Sulfolobus solfataricus; More
• Total number of polymer chains: 2
• Total formula weight: 18906.54

Authors

Chu, H.M.,Wang, A.H.J. (deposition date: 2006-08-29, release date: 2007-03-13, Last modification date: 2024-10-16)

Primary citation

Chu, H.M.,Wang, A.H.J.
Enzyme-substrate interactions revealed by the crystal structures of the archaeal Sulfolobus PTP-fold phosphatase and its phosphopeptide complexes
Proteins, 66:996-1003, 2006

PubMed Abstract: 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.

PubMed: 17173287
DOI: 10.1002/prot.21262

Experimental method

X-RAY DIFFRACTION (2.1 Å)