Crystallization and Preliminary X-ray Analysis of L-azetidine-2-carboxylate Hydrolase from Pseudomonas Sp. Strain A2C

Overview

Journal Acta Crystallogr Sect F Struct Biol Cryst Commun

Date 2010 Jul 8

PMID 20606277

Citations 2

Authors

Mayuko Toyoda

Keiji Jitsumori

Bunzo Mikami

Lawrence P Wackett

Tatsuo Kurihara

Nobuyoshi Esaki

Affiliations

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Abstract

L-Azetidine-2-carboxylate hydrolase from Pseudomonas sp. strain A2C catalyzes a ring-opening reaction that detoxifies L-azetidine-2-carboxylate, an analogue of L-proline. Recombinant L-azetidine-2-carboxylate hydrolase was overexpressed, purified and crystallized using polyethylene glycol and magnesium acetate as precipitants. The needle-shaped crystal belonged to space group P2(1), with unit-cell parameters a = 35.6, b = 63.6, c = 54.7 A, beta = 105.5 degrees . The crystal diffracted to a resolution of 1.38 A. The calculated V(M) value was 2.2 A(3) Da(-1), suggesting that the crystal contains one enzyme subunit in the asymmetric unit.

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