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. 2022 Apr 5;61(8):665–677. doi: 10.1021/acs.biochem.2c00080

Figure 9.

Figure 9

Closed and open structures of DBM and PHM. Left, two conformers of DBM with Cu atom (bronze) locations modeled (PDB file 4EZL). Middle: alignment of the protein fold of the closed crystal structure of H108A in the presence of citrate (PDB file 6ALA), with the open structure of the oxidized PHM (PDB file 1PHM). PHM structures were aligned on the N-terminal (H) subdomain with an RMSD value of 0.41. The H108A-citrate and the oxidized native PHM main chains are depicted by pink and purple ribbons, respectively. To emphasize the hinge motion, the first β-strands of the M-domains are colored green (closed: H108A-citrate) and dark blue (open: oxidized PHM). Right: enlarged view of the metal binding site in the H108A-citrate PHM structure. The single copper atom of the closed H108A-citrate structure, which coordinates M-site residues H242 and H244 and H-site residue H107, is shown in pink, while the citrate molecule is shown as a green carbon backbone with oxygen atoms in red. The positions of the two copper sites in the open PHM structure are shown as transparent slate spheres.