1ypt

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[[Image:1ypt.gif|left|200px]]
[[Image:1ypt.gif|left|200px]]
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{{Structure
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|PDB= 1ypt |SIZE=350|CAPTION= <scene name='initialview01'>1ypt</scene>, resolution 2.5&Aring;
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The line below this paragraph, containing "STRUCTURE_1ypt", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND=
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE= YOP51 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=630 Yersinia enterocolitica])
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|DOMAIN=
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{{STRUCTURE_1ypt| PDB=1ypt | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ypt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ypt OCA], [http://www.ebi.ac.uk/pdbsum/1ypt PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ypt RCSB]</span>
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'''CRYSTAL STRUCTURE OF YERSINIA PROTEIN TYROSINE PHOSPHATASE AT 2.5 ANGSTROMS AND THE COMPLEX WITH TUNGSTATE'''
'''CRYSTAL STRUCTURE OF YERSINIA PROTEIN TYROSINE PHOSPHATASE AT 2.5 ANGSTROMS AND THE COMPLEX WITH TUNGSTATE'''
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[[Category: Stuckey, J A.]]
[[Category: Stuckey, J A.]]
[[Category: Zhang, Z Y.]]
[[Category: Zhang, Z Y.]]
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[[Category: hydrolase]]
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[[Category: Hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:37:38 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:17:13 2008''
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Revision as of 13:37, 3 May 2008

Template:STRUCTURE 1ypt

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. 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 Page seeded by OCA on Sat May 3 16:37:38 2008

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