1ypt
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(New page: 200px<br /><applet load="1ypt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ypt, resolution 2.5Å" /> '''CRYSTAL STRUCTURE OF ...)
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Revision as of 04:51, 21 November 2007
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CRYSTAL STRUCTURE OF YERSINIA PROTEIN TYROSINE PHOSPHATASE AT 2.5 ANGSTROMS AND THE COMPLEX WITH TUNGSTATE
Overview
Protein tyrosine phosphatases (PTPases) and kinases coregulate the, critical levels of phosphorylation necessary for intracellular signalling, cell growth and differentiation. Yersinia, the causative bacteria of the, bubonic plague and other enteric diseases, secrete an active PTPase, Yop51, that enters and suppresses host immune cells. Though the catalytic, domain is only approximately 20% identical to human PTP1B, the Yersinia, PTPase contains all of the invariant residues present in eukaryotic, PTPases, including the nucleophilic Cys 403 which forms a phosphocysteine, intermediate during catalysis. We present here structures of the, unliganded (2.5 A resolution) and tungstate-bound (2.6 A) crystal forms, which reveal that Cys 403 is positioned at the centre of a distinctive, phosphate-binding loop. This loop is at the hub of several hydrogen-bond, arrays that not only stabilize a bound oxyanion, but may activate Cys 403, as a reactive thiolate. Binding of tungstate triggers a conformational, change that traps the oxyanion and swings Asp 356, an important catalytic, residue, by approximately 6 A into the active site. The same anion-binding, loop in PTPases is also found in the enzyme rhodanese.
About this Structure
1YPT is a Single protein structure of sequence from Yersinia enterocolitica. Active as Protein-tyrosine-phosphatase, with EC number 3.1.3.48 Full crystallographic information is available from OCA.
Reference
Crystal structure of Yersinia protein tyrosine phosphatase at 2.5 A and the complex with tungstate., Stuckey JA, Schubert HL, Fauman EB, Zhang ZY, Dixon JE, Saper MA, Nature. 1994 Aug 18;370(6490):571-5. PMID:8052312
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