1j97
From Proteopedia
Line 4: | Line 4: | ||
|PDB= 1j97 |SIZE=350|CAPTION= <scene name='initialview01'>1j97</scene>, resolution 1.5Å | |PDB= 1j97 |SIZE=350|CAPTION= <scene name='initialview01'>1j97</scene>, resolution 1.5Å | ||
|SITE= | |SITE= | ||
- | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> | + | |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> |
- | |ACTIVITY= [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] | + | |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> |
|GENE= | |GENE= | ||
+ | |DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=COG0560 SerB]</span> | ||
+ | |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.fli-leibniz.de/cgi-bin/ImgLib.pl?CODE=1kfv JenaLib], [http://www.rcsb.org/pdb/explore.do?structureId=1j97 RCSB]</span> | ||
}} | }} | ||
Line 33: | Line 35: | ||
[[Category: Yan, D.]] | [[Category: Yan, D.]] | ||
[[Category: Yokota, H.]] | [[Category: Yokota, H.]] | ||
- | [[Category: MG]] | ||
- | [[Category: PO4]] | ||
[[Category: berkeley structural genomics center]] | [[Category: berkeley structural genomics center]] | ||
[[Category: beryllium fluoride]] | [[Category: beryllium fluoride]] | ||
Line 45: | Line 45: | ||
[[Category: structural genomic]] | [[Category: structural genomic]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 26 05:53:54 2008'' |
Revision as of 03:53, 26 March 2008
| |||||||
, resolution 1.5Å | |||||||
---|---|---|---|---|---|---|---|
Ligands: | , , | ||||||
Activity: | Phosphoserine phosphatase, with EC number 3.1.3.3 | ||||||
Domains: | SerB | ||||||
Resources: | FirstGlance, OCA, PDBsum, JenaLib, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
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 Wed Mar 26 05:53:54 2008
Categories: Methanocaldococcus jannaschii | Phosphoserine phosphatase | Single protein | BSGC, Berkeley Structural Genomics Center. | Cho, H. | Damo, S. | Kim, R. | Kim, S H. | Kustu, S. | Wang, W. | Wemmer, D. | Yan, D. | Yokota, H. | Berkeley structural genomics center | Beryllium fluoride | Bsgc structure funded by nih | Phospho-aspartyl | Protein structure initiative | Psi | Psp | Structural genomic