Crystal structure of the protein At3g01520, a eukaryotic universal stress protein-like protein from arabidopsis thaliana in complex with AMP
- Seoul National Univ. (Korea)
- Georgian Court Univ., Lakewood, NJ (United States)
- Univ. of Wisconsin, Madison WI (United States)
- Chung-Ang Univ., Seoul (Korea)
- Univ. of Wisconsin, Madison, WI (United States); Rice Univ., Houston, TX (United States)
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.
- Research Organization:
- Argonne National Laboratory (ANL), Argonne, IL (United States)
- Sponsoring Organization:
- Future Planning of Korea; ICT; Ministry of Science; National Inst. of Health; USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22); USDOE Office of Science (SC), Biological and Environmental Research (BER) (SC-23)
- OSTI ID:
- 1247327
- Journal Information:
- Proteins, Journal Name: Proteins Journal Issue: 7 Vol. 83; ISSN 0887-3585
- Publisher:
- WileyCopyright Statement
- Country of Publication:
- United States
- Language:
- ENGLISH
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