Open AccessThe ybeY protein from Escherichia coli is a metalloprotein
Author(s) -
Zhan Chenyang,
Fedorov Elena V.,
Shi Wuxian,
Ramagopal U. A.,
Thirumuruhan R.,
Manjasetty Babu. A.,
Almo Steve C.,
Fiser Andras,
Chance Mark R.,
Fedorov Alexander A.
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309105031131
Subject(s) - structural genomics , metalloprotein , crystallography , escherichia coli , histidine , protein structure , structural bioinformatics , computational biology , chemistry , protein data bank , structural similarity , biology , biochemistry , enzyme , gene
The three‐dimensional crystallographic structure of the ybeY protein from Escherichia coli (SwissProt entry P77385) is reported at 2.7 Å resolution. YbeY is a hypothetical protein that belongs to the UPF0054 family. The structure reveals that the protein binds a metal ion in a tetrahedral geometry. Three coordination sites are provided by histidine residues, while the fourth might be a water molecule that is not seen in the diffraction map because of its relatively low resolution. X‐ray fluorescence analysis of the purified protein suggests that the metal is a nickel ion. The structure of ybeY and its sequence similarity to a number of predicted metal‐dependent hydrolases provides a functional assignment for this protein family. The figures and tables of this paper were prepared using semi‐automated tools, termed the Autopublish server, developed by the New York Structural GenomiX Research Consortium, with the goal of facilitating the rapid publication of crystallographic structures that emanate from worldwide Structural Genomics efforts, including the NIH‐funded Protein Structure Initiative.