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1j97

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[[Image:1j97.gif|left|200px]]
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{{Structure
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|PDB= 1j97 |SIZE=350|CAPTION= <scene name='initialview01'>1j97</scene>, resolution 1.5&Aring;
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|LIGAND= <scene name='pdbligand=BFD:ASPARTATE+BERYLLIUM+TRIFLUORIDE'>BFD</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoserine_phosphatase Phosphoserine phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.3 3.1.3.3] </span>
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{{STRUCTURE_1j97| PDB=1j97 | SCENE= }}
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|RELATEDENTRY=[[1f5s|1F5S]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1j97 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j97 OCA], [http://www.ebi.ac.uk/pdbsum/1j97 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1j97 RCSB]</span>
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'''Phospho-Aspartyl Intermediate Analogue of Phosphoserine phosphatase'''
'''Phospho-Aspartyl Intermediate Analogue of Phosphoserine phosphatase'''
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[[Category: Yan, D.]]
[[Category: Yan, D.]]
[[Category: Yokota, H.]]
[[Category: Yokota, H.]]
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[[Category: berkeley structural genomics center]]
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[[Category: Berkeley structural genomics center]]
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[[Category: beryllium fluoride]]
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[[Category: Beryllium fluoride]]
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[[Category: bsgc structure funded by nih]]
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[[Category: Bsgc structure funded by nih]]
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[[Category: phospho-aspartyl]]
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[[Category: Phospho-aspartyl]]
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[[Category: phosphoserine phosphatase]]
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[[Category: Phosphoserine phosphatase]]
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[[Category: protein structure initiative]]
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[[Category: Protein structure initiative]]
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[[Category: psi]]
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[[Category: Psi]]
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[[Category: psp]]
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[[Category: Psp]]
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[[Category: structural genomic]]
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Revision as of 17:56, 2 May 2008

Image:1j97.gif

Template:STRUCTURE 1j97

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.

About this Structure

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

Reference

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 Page seeded by OCA on Fri May 2 20:56:20 2008

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