1J97

Phospho-Aspartyl Intermediate Analogue of Phosphoserine phosphatase

Summary for 1J97

• Entry DOI: 10.2210/pdb1j97/pdb
• Related: 1F5S
• Descriptor: Phosphoserine Phosphatase, MAGNESIUM ION, PHOSPHATE ION, ... (4 entities in total)
• Functional Keywords: phosphoserine phosphatase, psp, phospho-aspartyl, beryllium fluoride, structural genomics, bsgc structure funded by nih, protein structure initiative, psi, berkeley structural genomics center, hydrolase
• Biological source: Methanocaldococcus jannaschii
• Total number of polymer chains: 2
• Total formula weight: 47637.87

Authors

Cho, H.,Wang, W.,Kim, R.,Yokota, H.,Damo, S.,Kim, S.-H.,Wemmer, D.,Kustu, S.,Yan, D.,Berkeley Structural Genomics Center (BSGC) (deposition date: 2001-05-24, release date: 2001-07-25, Last modification date: 2024-10-30)

Primary citation

Cho, H.,Wang, W.,Kim, R.,Yokota, H.,Damo, S.,Kim, S.-H.,Wemmer, D.,Kustu, S.,Yan, D.
BeF(3)(-) acts as a phosphate analog in proteins phosphorylated on aspartate: structure of a BeF(3)(-) complex with phosphoserine phosphatase.
Proc.Natl.Acad.Sci.USA, 98:8525-8530, 2001

PubMed Abstract: 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.

PubMed: 11438683
DOI: 10.1073/pnas.131213698

Experimental method

X-RAY DIFFRACTION (1.5 Å)