Crystallization and preliminary X-ray analysis of l-azetidine-2-carboxylate hydrolase from Pseudomonas sp. strain A2C

• Published in: Acta crystallographica. Section F, Structural biology and crystallization communications Vol. 66; no. 7; pp. 801 - 804
• Main Authors: Toyoda, Mayuko, Jitsumori, Keiji, Mikami, Bunzo, Wackett, Lawrence P., Kurihara, Tatsuo, Esaki, Nobuyoshi
• Format: Journal Article
• Language: English
• Published: 5 Abbey Square, Chester, Cheshire CH1 2HU, England International Union of Crystallography 01.06.2010
• Subjects: Amino Acid Sequence; Crystallization; Crystallization Communications; Crystallography, X-Ray; Hydrolases - chemistry; l-azetidine-2-carboxylate hydrolase; Molecular Sequence Data; Pseudomonas; Pseudomonas - enzymology; Pseudomonas sp. strain A2C; Sequence Alignment
• ISSN: 1744-3091; 1744-3091
• DOI: 10.1107/S1744309110017045

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 P21, with unit‐cell parameters a = 35.6, b = 63.6, c = 54.7 Å, β = 105.5°. The crystal diffracted to a resolution of 1.38 Å. The calculated VM value was 2.2 Å3 Da−1, suggesting that the crystal contains one enzyme subunit in the asymmetric unit.