1XFI

X-ray structure of gene product from Arabidopsis thaliana At2g17340

Summary for 1XFI

• Entry DOI: 10.2210/pdb1xfi/pdb
• Descriptor: unknown protein, MAGNESIUM ION (3 entities in total)
• Functional Keywords: structural genomics, protein structure initiative, psi, cesg, at2g17340, center for eukaryotic structural genomics, unknown function
• Biological source: Arabidopsis thaliana (thale cress)
• Total number of polymer chains: 1
• Total formula weight: 40905.03

Authors

Wesenberg, G.E.,Smith, D.W.,Phillips Jr., G.N.,Bitto, E.,Bingman, C.A.,Allard, S.T.M.,Center for Eukaryotic Structural Genomics (CESG) (deposition date: 2004-09-14, release date: 2004-09-28, Last modification date: 2024-02-14)

Primary citation

Bitto, E.,Bingman, C.A.,Allard, S.T.,Wesenberg, G.E.,Phillips, G.N.
The structure at 1.7 A resolution of the protein product of the At2g17340 gene from Arabidopsis thaliana.
Acta Crystallogr.,Sect.F, 61:630-635, 2005

PubMed Abstract: 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.

PubMed: 16511115
DOI: 10.1107/S1744309105017690

Experimental method

X-RAY DIFFRACTION (1.7 Å)