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Purification, crystallization and preliminary X-ray diffraction studies of a putative UDP-N-acetyl-D-mannosamine dehydrogenase from Pyrococcus horikoshii OT3.

ABSTRACT: A putative UDP-N-acetyl-D-mannosamine dehydrogenase from Pyrococcus horikoshii OT3, an essential enzyme for polysaccharide biosynthesis, has been overexpressed in Escherichia coli and purified. Crystals were obtained using the oil-microbatch method at 291 K. A native data set extending to 1.8 A resolution has been collected and processed in space group P2(1). Assuming the presence of a dimer in the asymmetric unit, the V(M) value is calculated to be 2.3 A3 Da(-1), which is consistent with the result of a dynamic light-scattering experiment that shows a dimeric state of the protein in solution.

SUBMITTER: Lokanath NK

PROVIDER: S-EPMC2334993 | biostudies-literature | 2007 May

REPOSITORIES: biostudies-literature

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Purification, crystallization and preliminary X-ray diffraction studies of a putative UDP-N-acetyl-D-mannosamine dehydrogenase from Pyrococcus horikoshii OT3.

Lokanath Neratur K NK Pampa Kudigana J KJ Kamiya Toshimi T Kunishima Naoki N

Acta crystallographica. Section F, Structural biology and crystallization communications 20070414 Pt 5

A putative UDP-N-acetyl-D-mannosamine dehydrogenase from Pyrococcus horikoshii OT3, an essential enzyme for polysaccharide biosynthesis, has been overexpressed in Escherichia coli and purified. Crystals were obtained using the oil-microbatch method at 291 K. A native data set extending to 1.8 A resolution has been collected and processed in space group P2(1). Assuming the presence of a dimer in the asymmetric unit, the V(M) value is calculated to be 2.3 A3 Da(-1), which is consistent with the re ...[more]

PMID: 17565184

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Pyrococcus horikoshii OT3

Project description:Anaerobic hyperthermophilic archeon

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