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Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 May 1; 63(Pt 5): 393–395.
Published online 2007 April 6. doi:  10.1107/S1744309107015102
PMCID: PMC2334997

Preliminary crystallographic analysis of l-2-keto-3-deoxyarabonate dehydratase, an enzyme involved in an alternative bacterial pathway of l-­arabinose metabolism

Naoko Shimada,a, Bunzo Mikami,b, Seiya Watanabe,a,c,d, and Keisuke Makinoa,c,e,*

Abstract

l-2-Keto-3-deoxyarabonate (l-KDA) dehydratase is a novel member of the dihydrodipicolinate synthase (DHDPS)/N-acetylneuraminate lyase (NAL) protein family and catalyzes the hydration of l-KDA to α-ketoglutaric semialdehyde. l-KDA dehydratase was overexpressed, purified and crystallized at 291 K using the hanging-drop vapour-diffusion method. The crystal diffracts to 2.0 Å resolution using synchrotron radiation and belongs to the trigonal space group P3121 or its enantiomorph P3221, with unit-cell parameters a = b = 78.91, c = 207.71 Å.

Keywords: l-2-Keto-3-deoxyarabonate dehydratase, dihydrodipicolinate synthase/N-acetylneuraminate lyase protein family

Articles from Acta Crystallographica Section F: Structural Biology and Crystallization Communications are provided here courtesy of International Union of Crystallography