Expression, Purification, Crystallization and Preliminary X-ray Studies of Histamine Dehydroganase from Nocardioides simplex
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Issue Date
2008-09-01Author
Reed, Timothy M.
Hirakawa, Hidehiko
Mure, Minae
Scott, Emily E.
Limburg, Julian
Publisher
International Union of Crystallography
Type
Article
Article Version
Scholarly/refereed, publisher version
Metadata
Show full item recordAbstract
Histamine dehydrogenase (HADH) from Nocardioides simplex catalyzes the oxidative deamination of histamine to produce imidazole acetaldehyde and an ammonium ion. HADH is functionally related to trimethylamine dehydrogenase (TMADH), but HADH has strict substrate specificity towards histamine. HADH is a homodimer, with each 76 kDa subunit containing two redox cofactors: a [4Fe-4S] cluster and an unusual covalently bound flavin mononucleotide, 6-S-cysteinyl-FMN. In order to understand the substrate specificity of HADH, it was sought to determine its structure by X-ray crystallography. This enzyme has been expressed recombinantly in Escherichia coli and successfully crystallized in two forms. Diffraction data were collected to 2.7 Å resolution at the SSRL synchrotron with 99.7% completeness. The crystals belonged to the orthorhombic space group P212121, with unit-cell parameters a = 101.14, b = 107.03, c = 153.35 Å.
Description
This is the publisher's version, also available electronically from http://scripts.iucr.org/cgi-bin/paper?S1744309108023336.
ISSN
1744-3091Collections
Citation
Reed, T. M.; Hirakawa, H.; Mure, Minae. "Expression, Purification, Crystallization and Preliminary X-ray Studies of Histamine Dehydroganase from Nocardioides simplex." Acta Crystallographica F, 64(9):785-787. http://www.dx.doi.org/10.1107/S1744309108023336.
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