6HWR

Red kidney bean purple acid phosphatase in complex with adenosine divanadate

「4KKZ」から置き換えられました

6HWR の概要

• エントリーDOI: 10.2210/pdb6hwr/pdb
• 分子名称: Fe(3+)-Zn(2+) purple acid phosphatase, TRIETHYLENE GLYCOL, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (19 entities in total)
• 機能のキーワード: purple acid phosphatase, metallohydrolases, transition state, catalysis, osteoporosis, metal binding protein
• 由来する生物種: Phaseolus vulgaris (Kidney bean); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 210461.13

構造登録者

Feder, D.,Gahan, L.R.,McGeary, R.P.,Guddat, L.W.,Schenk, G. (登録日: 2018-10-13, 公開日: 2019-04-03, 最終更新日: 2024-10-23)

主引用文献

Feder, D.,Gahan, L.R.,McGeary, R.P.,Guddat, L.W.,Schenk, G.
The Binding Mode of an ADP Analogue to a Metallohydrolase Mimics the Likely Transition State.
Chembiochem, 20:1536-1540, 2019

PubMed Abstract: Purple acid phosphatases (PAPs) are members of the large family of metallohydrolases, a group of enzymes that perform a wide range of biological functions, while employing a highly conserved catalytic mechanism. PAPs are found in plants, animals and fungi; in humans they play an important role in bone turnover and are thus of interest for developing treatments for osteoporosis. The majority of metallohydrolases use a metal-bound hydroxide to initiate catalysis, which leads to the formation of a proposed five-coordinate oxyphosphorane species in the transition state. In this work, we crystallized PAP from red kidney beans (rkbPAP) in the presence of both adenosine and vanadate. The in crystallo-formed vanadate analogue of ADP provides detailed insight into the binding mode of a PAP substrate, captured in a structure that mimics the putative fivecoordinate transition state. Our observations not only provide unprecedented insight into the mechanism of metallohydrolases, but might also guide the structure-based design of inhibitors for application in the treatment of several human illnesses.

PubMed: 30719821
DOI: 10.1002/cbic.201900077

実験手法

X-RAY DIFFRACTION (1.95 Å)