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Title: Expression, Purification, Crystallization And Preliminary X-Ray Studies of Histamine Dehydrogenase From Nocardioides Simplex

Abstract

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 {angstrom} resolution at the SSRL synchrotron with 99.7% completeness. The crystals belonged to the orthorhombic space group P2{sub 1}2{sub 1}2{sub 1}, with unit-cell parameters a = 101.14, b = 107.03, c = 153.35 {angstrom}.

Authors:
; ; ; ;
Publication Date:
Research Org.:
SLAC National Accelerator Lab., Menlo Park, CA (United States)
Sponsoring Org.:
USDOE
OSTI Identifier:
953059
Report Number(s):
SLAC-REPRINT-2009-225
TRN: US0902667
DOE Contract Number:  
AC02-76SF00515
Resource Type:
Journal Article
Journal Name:
Acta Crystallogr.F Struc.Biol.Crystalliz.Commun.64:785,2008
Additional Journal Information:
Journal Volume: 64; Journal Issue: 9
Country of Publication:
United States
Language:
English
Subject:
43 PARTICLE ACCELERATORS; ACETALDEHYDE; CRYSTALLIZATION; CRYSTALLOGRAPHY; DEAMINATION; DIFFRACTION; ENZYMES; ESCHERICHIA COLI; HISTAMINE; IMIDAZOLES; ISOALLOXAZINES; OXIDOREDUCTASES; PURIFICATION; RESOLUTION; SPACE GROUPS; SPECIFICITY; SUBSTRATES; SYNCHROTRONS; Other,OTHER, BIO

Citation Formats

Reed, T M, Hirakawa, H, Mure, M, Scott, E E, and Limburg, J. Expression, Purification, Crystallization And Preliminary X-Ray Studies of Histamine Dehydrogenase From Nocardioides Simplex. United States: N. p., 2009. Web.
Reed, T M, Hirakawa, H, Mure, M, Scott, E E, & Limburg, J. Expression, Purification, Crystallization And Preliminary X-Ray Studies of Histamine Dehydrogenase From Nocardioides Simplex. United States.
Reed, T M, Hirakawa, H, Mure, M, Scott, E E, and Limburg, J. 2009. "Expression, Purification, Crystallization And Preliminary X-Ray Studies of Histamine Dehydrogenase From Nocardioides Simplex". United States.
@article{osti_953059,
title = {Expression, Purification, Crystallization And Preliminary X-Ray Studies of Histamine Dehydrogenase From Nocardioides Simplex},
author = {Reed, T M and Hirakawa, H and Mure, M and Scott, E E and Limburg, J},
abstractNote = {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 {angstrom} resolution at the SSRL synchrotron with 99.7% completeness. The crystals belonged to the orthorhombic space group P2{sub 1}2{sub 1}2{sub 1}, with unit-cell parameters a = 101.14, b = 107.03, c = 153.35 {angstrom}.},
doi = {},
url = {https://www.osti.gov/biblio/953059}, journal = {Acta Crystallogr.F Struc.Biol.Crystalliz.Commun.64:785,2008},
number = 9,
volume = 64,
place = {United States},
year = {Thu May 21 00:00:00 EDT 2009},
month = {Thu May 21 00:00:00 EDT 2009}
}