Expression, purification and X-ray analysis of 1,3-propanediol dehydrogenase (Aq_1145) from Aquifex aeolicus VF5


Autoria(s): Jeyakanthan, Jeyaraman; Thamotharan, Subbiah; Panjikar, Santosh; Kitamura, Yoshiaki; Nakagawa, Noriko; Shinkai, Akeo; Kuramitsu, Seiki; Yokoyama, Shigeyuki
Data(s)

01/02/2010

Resumo

1,3-Propanediol dehydrogenase is an enzyme that catalyzes the oxidation of 1,3-propanediol to 3-hydroxypropanal with the simultaneous reduction of NADP(+) to NADPH. SeMet-labelled 1,3-propanediol dehydrogenase protein from the hyperthermophilic bacterium Aquifex aeolicus VF5 was overexpressed in Escherichia coli and purified to homogeneity. Crystals of this protein were grown from an acidic buffer with ammonium sulfate as the precipitant. Single-wavelength data were collected at the selenium peak to a resolution of 2.4 angstrom. The crystal belonged to space group P3(2), with unit-cell parameters a = b = 142.19, c = 123.34 angstrom. The structure contained two dimers in the asymmetric unit and was solved by the MR-SAD approach.

Formato

application/pdf

Identificador

http://eprints.iisc.ernet.in/25822/1/nj5048.pdf

Jeyakanthan, Jeyaraman and Thamotharan, Subbiah and Panjikar, Santosh and Kitamura, Yoshiaki and Nakagawa, Noriko and Shinkai, Akeo and Kuramitsu, Seiki and Yokoyama, Shigeyuki (2010) Expression, purification and X-ray analysis of 1,3-propanediol dehydrogenase (Aq_1145) from Aquifex aeolicus VF5. In: Acta Crystallographica Section F, 66 (Part 2). pp. 184-186.

Publicador

John Wiley and Sons

Relação

http://scripts.iucr.org/cgi-bin/paper?S1744309109052403

http://eprints.iisc.ernet.in/25822/

Palavras-Chave #Molecular Biophysics Unit
Tipo

Journal Article

PeerReviewed