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Proteins. 2015 Jul;83(7):1368-73. doi: 10.1002/prot.24821. Epub 2015 May 14.

Crystal structure of the protein At3g01520, a eukaryotic universal stress protein-like protein from Arabidopsis thaliana in complex with AMP.

Author information

1
Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University, Seoul, 151-742, Korea.
2
Department of Chemistry and Biochemistry, Georgian Court University, Lakewood, New Jersey, 08701.
3
Department of Biochemistry, Center for Eukaryotic Structural Genomics, University of Wisconsin-Madison, Madison, Wisconsin, 53706.
4
Laboratory of Stem Cell and Molecular Pharmacology, College of Pharmacy, Chung-Ang University, Seoul, 156-756, Korea.
5
BioSciences at Rice and Department of Chemistry, Rice University, Houston, Texas, 77251.

Abstract

Members of the universal stress protein (USP) family are conserved in a phylogenetically diverse range of prokaryotes, fungi, protists, and plants and confer abilities to respond to a wide range of environmental stresses. Arabidopsis thaliana contains 44 USP domain-containing proteins, and USP domain is found either in a small protein with unknown physiological function or in an N-terminal portion of a multi-domain protein, usually a protein kinase. Here, we report the first crystal structure of a eukaryotic USP-like protein encoded from the gene At3g01520. The crystal structure of the protein At3g01520 was determined by the single-wavelength anomalous dispersion method and refined to an R factor of 21.8% (Rfree = 26.1%) at 2.5 Å resolution. The crystal structure includes three At3g01520 protein dimers with one AMP molecule bound to each protomer, comprising a Rossmann-like α/β overall fold. The bound AMP and conservation of residues in the ATP-binding loop suggest that the protein At3g01520 also belongs to the ATP-binding USP subfamily members.

KEYWORDS:

Arabidopsis thaliana; At3g01520; universal stress protein

PMID:
25921306
PMCID:
PMC4624624
DOI:
10.1002/prot.24821
[Indexed for MEDLINE]
Free PMC Article

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