3RL4

Rat metallophosphodiesterase MPPED2 G252H Mutant

3RL4 の概要

• エントリーDOI: 10.2210/pdb3rl4/pdb
• 関連するPDBエントリー: 2HY0 2HY1 2HYP 3IB7 3IB8 3RL3 3RL5
• 分子名称: Metallophosphoesterase MPPED2, MANGANESE (II) ION, CHLORIDE ION, ... (6 entities in total)
• 機能のキーワード: alpha-beta fold, metallophosphodiesterase, active site mutant, gmp, hydrolase
• 由来する生物種: Rattus norvegicus (brown rat,rat,rats)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 34480.02

構造登録者

Podobnik, M.,Dermol, U. (登録日: 2011-04-19, 公開日: 2011-08-10, 最終更新日: 2024-02-28)

主引用文献

Dermol, U.,Janardan, V.,Tyagi, R.,Visweswariah, S.S.,Podobnik, M.
Unique utilization of a phosphoprotein phosphatase fold by a mammalian phosphodiesterase associated with WAGR syndrome.
J.Mol.Biol., 412:481-494, 2011

PubMed Abstract: Metallophosphoesterase-domain-containing protein 2 (MPPED2) is a highly evolutionarily conserved protein with orthologs found from worms to humans. The human MPPED2 gene is found in a region of chromosome 11 that is deleted in patients with WAGR (Wilms tumor, aniridia, genitourinary anomalies, and mental retardation) syndrome, and MPPED2 may function as a tumor suppressor. However, the precise cellular roles of MPPED2 are unknown, and its low phosphodiesterase activity suggests that substrate hydrolysis may not be its prime function. We present here the structures of MPPED2 and two mutants, which show that the poor activity of MPPED2 is not only a consequence of the substitution of an active-site histidine residue by glycine but also due to binding of AMP or GMP to the active site. This feature, enhanced by structural elements of the protein, allows MPPED2 to utilize the conserved phosphoprotein-phosphatase-like fold in a unique manner, ensuring that its enzymatic activity can be combined with a possible role as a scaffolding or adaptor protein.

PubMed: 21824479
DOI: 10.1016/j.jmb.2011.07.060

実験手法

X-RAY DIFFRACTION (1.29 Å)