Journal
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
Volume 90, Issue 5, Pages 1152-1158Publisher
WILEY
DOI: 10.1002/prot.26297
Keywords
disulfide bond; globins; ligand-binding site; neuroglobin; X-ray crystallography
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Funding
- National Natural Science Foundation of China [21977042, 21977017]
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This study elucidates the structure and function of human neuroglobin. By introducing an additional Cys residue, it was found that two disulfide bonds are formed. The binding of 1,4-dioxane from the crystallization reagents to both the protein and heme provides insights into protein-ligand interactions and guides the design of functional heme enzymes.
Human neuroglobin (Ngb) contains a heme group and three Cys residues (Cys46, Cys55, and Cys120) in the polypeptide chain. By introducing an additional Cys at position 15, the X-ray structure of A15C Ngb mutant was solved at a high resolution of 1.35 angstrom, which reveals the formation of both the native (C46-C55) and the engineered (C15-C120) disulfide bonds, likely playing a functional and structural role, respectively, according to the geometry analysis. Unexpectedly, 1,4-dioxane from the crystallization reagents was bound not only to the protein surface, but also to the heme distal pocket, providing insights into protein-ligand interactions for the globin and guiding the design of functional heme enzymes.
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