1j97: Difference between revisions

Revision as of 14:41, 1 July 2008

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File:1j97.png

Template:STRUCTURE 1j97

Phospho-Aspartyl Intermediate Analogue of Phosphoserine phosphatasePhospho-Aspartyl Intermediate Analogue of Phosphoserine phosphatase

Template:ABSTRACT PUBMED 11438683

About this StructureAbout this Structure

1J97 is a Single protein structure of sequence from Methanocaldococcus jannaschii. Full crystallographic information is available from OCA.

ReferenceReference

BeF(3)(-) acts as a phosphate analog in proteins phosphorylated on aspartate: structure of a BeF(3)(-) complex with phosphoserine phosphatase., Cho H, Wang W, Kim R, Yokota H, Damo S, Kim SH, Wemmer D, Kustu S, Yan D, Proc Natl Acad Sci U S A. 2001 Jul 17;98(15):8525-30. Epub 2001 Jul 3. PMID:11438683

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OCA

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-'''Phospho-Aspartyl Intermediate Analogue of Phosphoserine phosphatase'''
+===Phospho-Aspartyl Intermediate Analogue of Phosphoserine phosphatase===
-==Overview==
+<!--
-Protein phosphoaspartate bonds play a variety of roles. In response regulator proteins of two-component signal transduction systems, phosphorylation of an aspartate residue is coupled to a change from an inactive to an active conformation. In phosphatases and mutases of the haloacid dehalogenase (HAD) superfamily, phosphoaspartate serves as an intermediate in phosphotransfer reactions, and in P-type ATPases, also members of the HAD family, it serves in the conversion of chemical energy to ion gradients. In each case, lability of the phosphoaspartate linkage has hampered a detailed study of the phosphorylated form. For response regulators, this difficulty was recently overcome with a phosphate analog, BeF(3)(-), which yields persistent complexes with the active site aspartate of their receiver domains. We now extend the application of this analog to a HAD superfamily member by solving at 1.5-A resolution the x-ray crystal structure of the complex of BeF(3)(-) with phosphoserine phosphatase (PSP) from Methanococcus jannaschii. The structure is comparable to that of a phosphoenzyme intermediate: BeF(3)(-) is bound to Asp-11 with the tetrahedral geometry of a phosphoryl group, is coordinated to Mg(2+), and is bound to residues surrounding the active site that are conserved in the HAD superfamily. Comparison of the active sites of BeF(3)(-) x PSP and BeF(3)(-) x CeY, a receiver domain/response regulator, reveals striking similarities that provide insights into the function not only of PSP but also of P-type ATPases. Our results indicate that use of BeF(3)(-) for structural studies of proteins that form phosphoaspartate linkages will extend well beyond response regulators.
+The line below this paragraph, {{ABSTRACT_PUBMED_11438683}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11438683 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_11438683}}
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 [[Category: Psp]]
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