Crystal structure of the protein At3g01520, a eukaryotic universal stress protein-like protein from Arabidopsis thaliana in complex with AMP.
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 Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University, Seoul, 151-742, Korea.
Do Jin
DJ
Kim
Department of Chemistry and Biochemistry, Georgian Court University, Lakewood, New Jersey, 08701.
Eduard
E
Bitto
Department of Biochemistry, Center for Eukaryotic Structural Genomics, University of Wisconsin-Madison, Madison, Wisconsin, 53706.
Craig A
CA
Bingman
Laboratory of Stem Cell and Molecular Pharmacology, College of Pharmacy, Chung-Ang University, Seoul, 156-756, Korea.
Hyun-Jung
HJ
Kim
Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University, Seoul, 151-742, Korea.
Byung Woo
BW
Han
Department of Biochemistry, Center for Eukaryotic Structural Genomics, University of Wisconsin-Madison, Madison, Wisconsin, 53706.|BioSciences at Rice and Department of Chemistry, Rice University, Houston, Texas, 77251.
George N
GN
Phillips
D000249:Adenosine Monophosphate / Q000737:chemistry*; D000255:Adenosine Triphosphate / Q000737:chemistry*; D000595:Amino Acid Sequence; D017360:Arabidopsis / Q000737:chemistry* / Q000378:metabolism; D029681:Arabidopsis Proteins / Q000737:chemistry* / Q000235:genetics; D001665:Binding Sites; D017124:Conserved Sequence; D018360:Crystallography, X-Ray; D015870:Gene Expression; D006360:Heat-Shock Proteins / Q000737:chemistry* / Q000235:genetics; D057927:Hydrophobic and Hydrophilic Interactions; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011485:Protein Binding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics; D016415:Sequence Alignment
D029681:Arabidopsis Proteins; D006360:Heat-Shock Proteins; D011994:Recombinant Proteins; D000249:Adenosine Monophosphate; D000255:Adenosine Triphosphate
Arabidopsis thaliana; At3g01520; universal stress protein