1l7n

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spinqualitylabelsall models 1l7n, resolution 1.8Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

TRANSITION STATE ANALOGUE OF PHOSPHOSERINE PHOSPHATASE (ALUMINUM FLUORIDE COMPLEX)

Overview

Phosphoserine phosphatase (PSP) is a member of a large class of enzymes, that catalyze phosphoester hydrolysis using a phosphoaspartate-enzyme, intermediate. PSP is a likely regulator of the steady-state d-serine level, in the brain, which is a critical co-agonist of the N-methyl-d-aspartate, type of glutamate receptors. Here, we present high-resolution (1.5-1.9 A), structures of PSP from Methanococcus jannaschii, which define the open, state prior to substrate binding, the complex with phosphoserine substrate, bound (with a D to N mutation in the active site), and the complex with, AlF3, a transition-state analog for the phospho-transfer steps in the, reaction. These structures, together with those described for the BeF3-, complex (mimicking the phospho-enzyme) and the enzyme with phosphate, product in the active site, provide a detailed structural picture of the, full reaction cycle. The structure of the apo state indicates partial, unfolding of the enzyme to allow substrate binding, with refolding in the, presence of substrate to provide specificity. Interdomain and active-site, conformational changes are identified. The structure with the transition, state analog bound indicates a "tight" intermediate. A striking structure, homology, with significant sequence conservation, among PSP, P-type, ATPases and response regulators suggests that the knowledge of the PSP, reaction mechanism from the structures determined will provide insights, into the reaction mechanisms of the other enzymes in this family.

About this Structure

1L7N is a Single protein structure of sequence from Methanocaldococcus jannaschii with ALF, MG, SO4 and AF3 as ligands. Active as Phosphoserine phosphatase, with EC number 3.1.3.3 Full crystallographic information is available from OCA.

Reference

Structural characterization of the reaction pathway in phosphoserine phosphatase: crystallographic "snapshots" of intermediate states., Wang W, Cho HS, Kim R, Jancarik J, Yokota H, Nguyen HH, Grigoriev IV, Wemmer DE, Kim SH, J Mol Biol. 2002 May 31;319(2):421-31. PMID:12051918

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