The structure at 1.7 A resolution of the protein product of the At2g17340 gene from Arabidopsis thaliana.
The crystal structure of the At2g17340 protein from A. thaliana was determined by the multiple-wavelength anomalous diffraction method and was refined to an R factor of 16.9% (Rfree = 22.1%) at 1.7 A resolution. At2g17340 is a member of the Pfam01937.11 protein family and its structure provides the first insight into the structural organization of this family. A number of fully and highly conserved residues defined by multiple sequence alignment of members of the Pfam01937.11 family were mapped onto the structure of At2g17340. The fully conserved residues are involved in the coordination of a metal ion and in the stabilization of loops surrounding the metal site. Several additional highly conserved residues also map into the vicinity of the metal-binding site, while others are clearly involved in stabilizing the hydrophobic core of the protein. The structure of At2g17340 represents a new fold in protein conformational space.
Bitto
Eduard
E
Center for Eukaryotic Structural Genomics, Department of Biochemistry, University of Wisconsin-Madison, USA.
Bingman
Craig A
CA
Allard
Simon T M
ST
Wesenberg
Gary E
GE
Phillips
George N
GN
D000595:Amino Acid Sequence; D017360:Arabidopsis / Q000378:metabolism*; D001665:Binding Sites; D002384:Catalysis; D003001:Cloning, Molecular; D017124:Conserved Sequence; D018360:Crystallography, X-Ray; D007477:Ions; D008670:Metals; D008958:Models, Molecular; D008968:Molecular Conformation; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid; D014961:X-Ray Diffraction
D007477:Ions; D008670:Metals