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Crystallization (Commentary)
1.13.11.19
structure of cysteamine dioxygenase at 1.9 A resolution, an Fe and three-histidine (3-His) active site is situated at the end of a wide substrate access channel. Whole-protein models of ADO in complex with either cysteamine or an N-terminal-Cys peptide suggest occlusion of access to the active site by peptide substrate binding. A small tunnel that leads from the opposite face of the enzyme into the active site provides a path through which co-substrate O2 can access the Fe center. The entrance to the tunnel is guarded by two Cys residues that may form a disulfide bond to regulate O2 delivery
1.13.11.19
structure of human ADO at a resolution of 1.78 A with a nickel-bound metal center. Crystallization is achieved through both metal substitution and C18S/C239S double mutations. The metal center resides in a tunnel close to an entry site flanked by loops. ADO appears to use extensive flexibility to handle substrates of different sizes, and also employs proline and proline pairs to maintain the core protein structure and to retain the residues critical for catalysis in place
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