6HYY

Human phosphoserine phosphatase with serine and phosphate

6HYY の概要

• エントリーDOI: 10.2210/pdb6hyy/pdb
• 分子名称: Phosphoserine phosphatase, PHOSPHATE ION, MAGNESIUM ION, ... (6 entities in total)
• 機能のキーワード: human phosphoserine phosphatase, hydrolase
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 49525.66

構造登録者

Wouters, J.,Haufroid, M.,Mirgaux, M. (登録日: 2018-10-22, 公開日: 2019-06-12, 最終更新日: 2024-01-24)

主引用文献

Haufroid, M.,Mirgaux, M.,Leherte, L.,Wouters, J.
Crystal structures and snapshots along the reaction pathway of human phosphoserine phosphatase.
Acta Crystallogr D Struct Biol, 75:592-604, 2019

PubMed Abstract: The equilibrium between phosphorylation and dephosphorylation is one of the most important processes that takes place in living cells. Human phosphoserine phosphatase (hPSP) is a key enzyme in the production of serine by the dephosphorylation of phospho-L-serine. It is directly involved in the biosynthesis of other important metabolites such as glycine and D-serine (a neuromodulator). hPSP is involved in the survival mechanism of cancer cells and has recently been found to be an essential biomarker. Here, three new high-resolution crystal structures of hPSP (1.5-2.0 Å) in complexes with phosphoserine and with serine, which are the substrate and the product of the reaction, respectively, and in complex with a noncleavable substrate analogue (homocysteic acid) are presented. New types of interactions take place between the enzyme and its ligands. Moreover, the loop involved in the open/closed state of the enzyme is fully refined in a totally unfolded conformation. This loop is further studied through molecular-dynamics simulations. Finally, all of these analyses allow a more complete reaction mechanism for this enzyme to be proposed which is consistent with previous publications on the subject.

PubMed: 31205021
DOI: 10.1107/S2059798319006867

実験手法

X-RAY DIFFRACTION (1.566 Å)