2GM3

Crystal Structure of an Universal Stress Protein Family Protein from Arabidopsis Thaliana At3g01520 with AMP Bound

Summary for 2GM3

• Entry DOI: 10.2210/pdb2gm3/pdb
• Descriptor: unknown protein, ADENOSINE MONOPHOSPHATE (3 entities in total)
• Functional Keywords: at3g01520, putative ethylene-responsive protein, usp domain, nucleotide binding domain, amp, protein structure initiative, psi, center for eukaryotic structural genomics, cesg, structural genomics, unknown function
• Biological source: Arabidopsis thaliana (thale cress)
• Total number of polymer chains: 6
• Total formula weight: 120234.93

Authors

Bitto, E.,Wesenberg, G.E.,Phillips Jr., G.N.,Bingman, C.A.,Center for Eukaryotic Structural Genomics (CESG) (deposition date: 2006-04-05, release date: 2006-04-18, Last modification date: 2024-10-16)

Primary citation

Kim, D.O.J.,Bitto, E.,Bingman, C.A.,Kim, H.J.,Han, B.W.,Phillips, G.N.
Crystal structure of the protein At3g01520, a eukaryotic universal stress protein-like protein from arabidopsis thaliana in complex with AMP.
Proteins, 83:1368-1373, 2015

PubMed 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.

PubMed: 25921306
DOI: 10.1002/prot.24821

Experimental method

X-RAY DIFFRACTION (2.461 Å)