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1j97
From Proteopedia
(New page: 200px<br /><applet load="1j97" size="450" color="white" frame="true" align="right" spinBox="true" caption="1j97, resolution 1.5Å" /> '''Phospho-Aspartyl Inte...) |
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| - | [[Image:1j97.gif|left|200px]]<br /><applet load="1j97" size=" | + | [[Image:1j97.gif|left|200px]]<br /><applet load="1j97" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1j97, resolution 1.5Å" /> | caption="1j97, resolution 1.5Å" /> | ||
'''Phospho-Aspartyl Intermediate Analogue of Phosphoserine phosphatase'''<br /> | '''Phospho-Aspartyl Intermediate Analogue of Phosphoserine phosphatase'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Protein phosphoaspartate bonds play a variety of roles. In response | + | 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== | ==About this Structure== | ||
| - | 1J97 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii] with MG and PO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http:// | + | 1J97 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=PO4:'>PO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J97 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Phosphoserine phosphatase]] | [[Category: Phosphoserine phosphatase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: BSGC, Berkeley | + | [[Category: BSGC, Berkeley Structural Genomics Center.]] |
[[Category: Cho, H.]] | [[Category: Cho, H.]] | ||
[[Category: Damo, S.]] | [[Category: Damo, S.]] | ||
[[Category: Kim, R.]] | [[Category: Kim, R.]] | ||
| - | [[Category: Kim, S | + | [[Category: Kim, S H.]] |
[[Category: Kustu, S.]] | [[Category: Kustu, S.]] | ||
[[Category: Wang, W.]] | [[Category: Wang, W.]] | ||
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[[Category: structural genomics]] | [[Category: structural genomics]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:20:02 2008'' |
Revision as of 11:20, 21 February 2008
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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 with and as ligands. Active as Phosphoserine phosphatase, with EC number 3.1.3.3 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 Thu Feb 21 13:20:02 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. | MG | PO4 | Berkeley structural genomics center | Beryllium fluoride | Bsgc structure funded by nih | Phospho-aspartyl | Protein structure initiative | Psi | Psp | Structural genomics
