2i6j: Difference between revisions

Revision as of 17:09, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2i6j.png

Template:STRUCTURE 2i6j

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

Template:ABSTRACT PUBMED 17173287

About this StructureAbout this Structure

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

ReferenceReference

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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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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 {{STRUCTURE_2i6j|  PDB=2i6j  |  SCENE=  }}
-'''Crystal structure of the complex of the archaeal sulfolobus PTP-fold phosphatase with phosphate ion'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_17173287}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17173287 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17173287}}
 ==About this Structure==
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 [[Category: Wang, A H.J.]]
 [[Category: Ptp domain]]
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