Crystal structure of the protein At3g01520, a eukaryotic universal stress protein‐like protein from arabidopsis thaliana in complex with AMP |
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| Authors: | Craig A Bingman Hyun‐Jung Kim Byung Woo Han George N Phillips Jr |
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| Institution: | 1. Department of Biochemistry, Center for Eukaryotic Structural Genomics, University of Wisconsin‐Madison, Madison, Wisconsin;2. Laboratory of Stem Cell and Molecular Pharmacology, College of Pharmacy, Chung‐Ang University, Seoul, Korea;3. Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University, Seoul, Korea;4. BioSciences at Rice and Department of Chemistry, Rice University, Houston, Texas |
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| 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. Proteins 2015; 83:1368–1373. © 2015 The Authors. Proteins: Structure, Function, and Bioinformatics Published by Wiley Periodicals, Inc. |
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| Keywords: | universal stress protein Arabidopsis thaliana At3g01520 |
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