2QQC

E109Q mutant of Pyruvoyl-dependent Arginine Decarboxylase from Methanococcus jannashii

2QQC の概要

• エントリーDOI: 10.2210/pdb2qqc/pdb
• 関連するPDBエントリー: 2QQD
• 分子名称: Pyruvoyl-dependent arginine decarboxylase subunit beta, Pyruvoyl-dependent arginine decarboxylase subunit alpha, AGMATINE, ... (5 entities in total)
• 機能のキーワード: arginine decarboxylase, pyruvoyl, decarboxylation, autoprocessing, serinolysis, lyase, pyruvate
• 由来する生物種: Methanocaldococcus jannaschii; 詳細
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 108430.01

構造登録者

Ealick, S.E.,Soriano, E.S. (登録日: 2007-07-26, 公開日: 2008-03-18, 最終更新日: 2024-10-16)

主引用文献

Soriano, E.V.,McCloskey, D.E.,Kinsland, C.,Pegg, A.E.,Ealick, S.E.
Structures of the N47A and E109Q mutant proteins of pyruvoyl-dependent arginine decarboxylase from Methanococcus jannaschii.
Acta Crystallogr.,Sect.D, 64:377-382, 2008

PubMed Abstract: Pyruvoyl-dependent arginine decarboxylase (PvlArgDC) catalyzes the first step of the polyamine-biosynthetic pathway in plants and some archaebacteria. The pyruvoyl group of PvlArgDC is generated by an internal autoserinolysis reaction at an absolutely conserved serine residue in the proenzyme, resulting in two polypeptide chains. Based on the native structure of PvlArgDC from Methanococcus jannaschii, the conserved residues Asn47 and Glu109 were proposed to be involved in the decarboxylation and autoprocessing reactions. N47A and E109Q mutant proteins were prepared and the three-dimensional structure of each protein was determined at 2.0 A resolution. The N47A and E109Q mutant proteins showed reduced decarboxylation activity compared with the wild-type PvlArgDC. These residues may also be important for the autoprocessing reaction, which utilizes a mechanism similar to that of the decarboxylation reaction.

PubMed: 18391404
DOI: 10.1107/S0907444908000474

実験手法

X-RAY DIFFRACTION (2 Å)