3ML0

Thermostable Penicillin G acylase from Alcaligenes faecalis in tetragonal form

3ML0 の概要

• エントリーDOI: 10.2210/pdb3ml0/pdb
• 関連するPDBエントリー: 3K3W
• 分子名称: Penicillin G acylase, alpha subunit, Penicillin G acylase, beta subunit, CALCIUM ION (3 entities in total)
• 機能のキーワード: penicillin g acylase, hydrolase
• 由来する生物種: Alcaligenes faecalis; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 85090.92

構造登録者

Varshney, N.K.,Kumar, R.S.,Ignatova, Z.,Dodson, E.,Suresh, C.G. (登録日: 2010-04-16, 公開日: 2010-05-05, 最終更新日: 2024-10-09)

主引用文献

Varshney, N.K.,Kumar, R.S.,Ignatova, Z.,Prabhune, A.,Pundle, A.,Dodson, E.,Suresh, C.G.
Crystallization and X-ray structure analysis of a thermostable penicillin G acylase from Alcaligenes faecalis.
Acta Crystallogr.,Sect.F, 68:273-277, 2012

PubMed Abstract: The enzyme penicillin G acylase (EC 3.5.1.11) catalyzes amide-bond cleavage in benzylpenicillin (penicillin G) to yield 6-aminopenicillanic acid, an intermediate chemical used in the production of semisynthetic penicillins. A thermostable penicillin G acylase from Alcaligenes faecalis (AfPGA) has been crystallized using the hanging-drop vapour-diffusion method in two different space groups: C222(1), with unit-cell parameters a = 72.9, b = 86.0, c = 260.2 , and P4(1)2(1)2, with unit-cell parameters a = b = 85.6, c = 298.8 . Data were collected at 293 and the structure was determined using the molecular-replacement method. Like other penicillin acylases, AfPGA belongs to the N-terminal nucleophilic hydrolase superfamily, has undergone post-translational processing and has a serine as the N-terminal residue of the β-chain. A disulfide bridge has been identified in the structure that was not found in the other two known penicillin G cylase structures. The presence of the disulfide bridge is perceived to be one factor that confers higher stability to this enzyme.

PubMed: 22442220
DOI: 10.1107/S1744309111053930

実験手法

X-RAY DIFFRACTION (3.5 Å)