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

Journal Article · Tue May 01 00:00:00 EDT 2007 · Acta Crystallographica. Section F

DOI:https://doi.org/10.1107/S1744309107015102· OSTI ID:22360321

Shimada, Naoko ^[1]; Mikami, Bunzo ^[2]; Watanabe, Seiya ^[1]; Makino, Keisuke ^[1]

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1. Institute of Advanced Energy, Kyoto University, Gokasyo, Uji, Kyoto 611-0011 (Japan)
2. Laboratory of Applied Structural Biology, Division of Applied Life Science, Graduate School of Agriculture, Kyoto University, Gokasyo, Uji, Kyoto 611-0011 (Japan)

l-2-Keto-3-deoxyarabonate dehydratase was overexpressed, purified and crystallized at 291 K using the hanging-drop vapour-diffusion method. 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 P3{sub 1}21 or its enantiomorph P3{sub 2}21, with unit-cell parameters a = b = 78.91, c = 207.71 Å.

• OSTI ID: 22360321
• Journal Information: Acta Crystallographica. Section F, Vol. 63, Issue Pt 5; Other Information: PMCID: PMC2334997; PMID: 17565178; PUBLISHER-ID: en5228; OAI: oai:pubmedcentral.nih.gov:2334997; Copyright (c) International Union of Crystallography 2007; This is an open-access article distributed under the terms described at http://journals.iucr.org/services/termsofuse.html.; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
• Country of Publication: United Kingdom
• Language: English

Related Subjects

75 CONDENSED MATTER PHYSICS
SUPERCONDUCTIVITY AND SUPERFLUIDITY
CRYSTALS
DIFFUSION
HYDRATION
RESOLUTION
SPACE GROUPS
SYNCHROTRON RADIATION