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Crystallization and preliminary crystallographic analysis of N-acetyltransferase Mpr1 from Saccharomyces cerevisiae.
- Source :
-
Acta crystallographica. Section F, Structural biology and crystallization communications [Acta Crystallogr Sect F Struct Biol Cryst Commun] 2009 Feb 01; Vol. 65 (Pt 2), pp. 169-72. Date of Electronic Publication: 2009 Jan 31. - Publication Year :
- 2009
-
Abstract
- Mpr1 is an enzyme that catalyzes the N-acetylation of the toxic L-azetidine-2-carboxylic acid (AZC). Recently, Mpr1 has been shown to reduce levels of intracellular reactive oxygen species (ROS) under oxidative stress. The natural substrate involved in the ROS elimination in vivo is still unknown. Mpr1 has been purified and crystallized in space groups P1 and P3(1)12. X-ray data were collected to 1.9 A resolution from a trigonal crystal soaked with AZC.
- Subjects :
- Acetyltransferases genetics
Amino Acid Sequence
Catalytic Domain genetics
Crystallization
Crystallography, X-Ray
Molecular Sequence Data
Saccharomyces cerevisiae genetics
Saccharomyces cerevisiae Proteins genetics
Substrate Specificity genetics
Acetyltransferases chemistry
Saccharomyces cerevisiae enzymology
Saccharomyces cerevisiae Proteins chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 1744-3091
- Volume :
- 65
- Issue :
- Pt 2
- Database :
- MEDLINE
- Journal :
- Acta crystallographica. Section F, Structural biology and crystallization communications
- Publication Type :
- Academic Journal
- Accession number :
- 19194013
- Full Text :
- https://doi.org/10.1107/S1744309109000153