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. 2006 Jun 1;63(4):1097-101.
doi: 10.1002/prot.20589.

Crystal structure of hypothetical protein YfiH from Shigella flexneri at 2 A resolution

Youngchang Kim  1 , Natalia Maltseva, Irina Dementieva, Frank Collart, Denise Holzle, Andrzej Joachimiak
Affiliations

Crystal structure of hypothetical protein YfiH from Shigella flexneri at 2 A resolution

Youngchang Kim et al. Proteins. .
No abstract available

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Figures

Fig. 1
Fig. 1
Crystal structure of YfiH protein. A: Ribbon diagram of YfiH protein. Helices are shown in blue, β-sheets in red, and Zn2 + ions are indicated in magenta; orange indicates protein residues interacting with Zn2+ ions, among eight Zn2+ ions in the asymmetric unit, six Zn2+ ions are shown here, four of these are shared between the two protein molecules. The two Zn2 + ions not shown interact with the other protein molecule in the asymmetric unit. Secondary structure elements are also indicated in black. B: Diagram showing the secondary structure elements in YfiH protein superimposed on its primary sequence. Residues interacting with Zn2+ ions are marked with blue dots and residues interacting with acetate molecules are marked with red. β-Hairpins are depicted as red loops. C: The potential active site of YfiH protein. The Zn2 + ions are coordinated to an acetate molecule, a cysteine and two histidine residues forming a tetrahedral configuration.
Fig. 2
Fig. 2
Multiple sequence alignment of YfiH protein homologs from various species. AAP17973.1 (Shigella flexneri), NP_754996.1 (Escherichia coli), NP_461592.1 (Salmonella typhimurium), AB0832 (Salmonella enterica subsp enterica), ZP_00156016.2 (Haemophilis influenzae), CAG13296.1 (Tetraodon nigroviridis), AAH78069.1 (Xenopus laevis), XP_233749.1 (Ratus norwegicus), AAH35749.1 (Homo sapiens), XP_417036.1 (Gallus gallus), NP_766076.1 (Mus musculus). Idt, percentage of identity. The conservations of His-71, Cys-107, and His-124, and identical amino acids are shown in red and blue, respectively.
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