2i6j

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|PDB= 2i6j |SIZE=350|CAPTION= <scene name='initialview01'>2i6j</scene>, resolution 1.66&Aring;
|PDB= 2i6j |SIZE=350|CAPTION= <scene name='initialview01'>2i6j</scene>, resolution 1.66&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=PO4:PHOSPHATE ION'>PO4</scene>
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|LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>
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|ACTIVITY= [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]
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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>
|GENE=
|GENE=
 +
|DOMAIN=
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|RELATEDENTRY=[[2dxp|2DXP]], [[2i6i|2I6I]], [[2i6m|2I6M]], [[2i6o|2I6O]], [[2i6p|2I6P]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2i6j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i6j OCA], [http://www.ebi.ac.uk/pdbsum/2i6j PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2i6j RCSB]</span>
}}
}}
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[[Category: Chu, H M.]]
[[Category: Chu, H M.]]
[[Category: Wang, A H.J.]]
[[Category: Wang, A H.J.]]
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[[Category: PO4]]
 
[[Category: ptp domain]]
[[Category: ptp domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:26:03 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:40:23 2008''

Revision as of 00:40, 31 March 2008


PDB ID 2i6j

Drag the structure with the mouse to rotate
, resolution 1.66Å
Ligands:
Activity: Protein-tyrosine-phosphatase, with EC number 3.1.3.48
Related: 2DXP, 2I6I, 2I6M, 2I6O, 2I6P


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Crystal structure of the complex of the archaeal sulfolobus PTP-fold phosphatase with phosphate ion


Overview

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.

About this Structure

2I6J is a Single protein structure of sequence from Sulfolobus solfataricus. Full crystallographic information is available from OCA.

Reference

Enzyme-substrate interactions revealed by the crystal structures of the archaeal Sulfolobus PTP-fold phosphatase and its phosphopeptide complexes., Chu HM, Wang AH, Proteins. 2007 Mar 1;66(4):996-1003. PMID:17173287

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