Open AccessThe structure at 1.7 Å resolution of the protein product of the At2g17340 gene from Arabidopsis thaliana
Author(s) -
Bitto Eduard,
Bingman Craig A.,
Allard Simon T. M.,
Wesenberg Gary E.,
Phillips George N.
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309105017690
Subject(s) - structural genomics , arabidopsis thaliana , crystallography , crystal structure , chemistry , protein structure , resolution (logic) , metal , molecular replacement , stereochemistry , gene , biochemistry , mutant , artificial intelligence , computer science , organic chemistry
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% ( R free = 22.1%) at 1.7 Å 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.