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Title: Crystal structure of the protein At3g01520, a eukaryotic universal stress protein-like protein from arabidopsis thaliana in complex with AMP

Journal Article · · Proteins
DOI:https://doi.org/10.1002/prot.24821· OSTI ID:1247327
 [1];  [2];  [3];  [4];  [1];  [5]
  1. Seoul National Univ. (Korea)
  2. Georgian Court Univ., Lakewood, NJ (United States)
  3. Univ. of Wisconsin, Madison WI (United States)
  4. Chung-Ang Univ., Seoul (Korea)
  5. Univ. of Wisconsin, Madison, WI (United States); Rice Univ., Houston, TX (United States)
+ Show Author Affiliations

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:
USDOE Office of Science (SC), Biological and Environmental Research (BER); USDOE Office of Science (SC), Basic Energy Sciences (BES); National Inst. of Health; Ministry of Science; ICT; Future Planning of Korea
Grant/Contract Number:
U01 GM098248; U54 GM074901; P50 GM64598; 2011‐0030001; 2013M3A6A4043695
OSTI ID:
1247327
Journal Information:
Proteins, Vol. 83, Issue 7; ISSN 0887-3585
Publisher:
WileyCopyright Statement
Country of Publication:
United States
Language:
ENGLISH
Citation Metrics:
Cited by: 10 works
Citation information provided by
Web of Science

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Cited By (3)

Virus-induced gene silencing of the RPC5-like subunit of RNA polymerase III caused pleiotropic effects in Nicotiana benthamiana journal June 2016
PZQ Therapy: How Close are we in the Development of Effective Alternative Anti-schistosomal Drugs? journal December 2019
Universal Stress Proteins as New Targets for Environmental and Therapeutic Interventions of Schistosomiasis journal September 2016

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59 BASIC BIOLOGICAL SCIENCES
universal stress protein
Arabidopsis thaliana
At3g01520