3WYO

Heterodimeric myoglobin formed by domain swapping

Summary for 3WYO

• Entry DOI: 10.2210/pdb3wyo/pdb
• Related: 3VM9
• Descriptor: Myoglobin, PROTOPORPHYRIN IX CONTAINING FE, ... (4 entities in total)
• Functional Keywords: globin, oxygen binding
• Biological source: Equus caballus (horse); More
• Total number of polymer chains: 4
• Total formula weight: 70400.00

Authors

Lin, Y.W.,Nagao, S.,Zhang, M.,Shomura, Y.,Higuchi, Y.,Hirota, S. (deposition date: 2014-09-04, release date: 2014-11-19, Last modification date: 2023-11-08)

Primary citation

Lin, Y.W.,Nagao, S.,Zhang, M.,Shomura, Y.,Higuchi, Y.,Hirota, S.
Rational design of heterodimeric protein using domain swapping for myoglobin.
Angew.Chem.Int.Ed.Engl., 54:511-515, 2015

PubMed Abstract: Protein design is a useful method to create novel artificial proteins. A rational approach to design a heterodimeric protein using domain swapping for horse myoglobin (Mb) was developed. As confirmed by X-ray crystallographic analysis, a heterodimeric Mb with two different active sites was produced efficiently from two surface mutants of Mb, in which the charges of two amino acids involved in the dimer salt bridges were reversed in each mutant individually, with the active site of one mutant modified. This study shows that the method of constructing heterodimeric Mb with domain swapping is useful for designing artificial multiheme proteins.

PubMed: 25370865
DOI: 10.1002/anie.201409267

Experimental method

X-RAY DIFFRACTION (2 Å)