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Figure 1
Arrangement of YfeA protomers and crystallographic packing. YfeA protomers are colored in a spectrum from blue (amino-terminus) to red (carboxy-terminus) and metals are shown as spheres. (a) Site 1 is a buried metal-binding site with four amino-acid ligands and site 2 is a surface site with two amino-acid ligands. Anomalous difference electron density contoured at 4σ (magenta mesh) shows the location of each metal. (b) Two YfeA protomers are present in the asymmetric unit of each crystal and the site 2 motifs are distant from each other. (c) Each protomer interacts with two symmetry-related protomers (shown as transparent molecules) to form a crystallographic complex. In the arrangement shown, two site 2 motifs (green) flank residues from a His10 tag (red). The protomers in the complex are related by rotation and reflection symmetry along the screw axis. Blocks colored according to the YfeA sequence show the symmetry relationship between protomers and how the metal is wedged between protomers. (d) Overview of the positional distribution of metals in the YfeA crystal packing. A metal is present in site 1 in all structures. PDB entries 5uyg and 5uyh show the canonical site 2 metal site. Metals present in YfeA site 2 inter-coordinated structure 1, structure 2 and structure 3 are denoted 1, 2 and 3, respectively. A common metal is present in structures 2 and 3.

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X
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