6LTL
The dimeric structure of G80A myoglobin
Summary for 6LTL
| Entry DOI | 10.2210/pdb6ltl/pdb |
| Related | 6LS8 |
| Descriptor | Myoglobin, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total) |
| Functional Keywords | oxygen storage, oxygen binding |
| Biological source | Equus caballus (Horse) |
| Total number of polymer chains | 2 |
| Total formula weight | 35228.05 |
| Authors | Nagao, S.,Suda, A.,Kobayashi, H.,Shibata, N.,Higuchi, Y.,Hirota, S. (deposition date: 2020-01-22, release date: 2020-05-06, Last modification date: 2023-11-29) |
| Primary citation | Nagao, S.,Suda, A.,Kobayashi, H.,Shibata, N.,Higuchi, Y.,Hirota, S. Thermodynamic Control of Domain Swapping by Modulating the Helical Propensity in the Hinge Region of Myoglobin. Chem Asian J, 15:1743-1749, 2020 Cited by PubMed Abstract: Domain swapping is an exception to Anfinsen's dogma, and more than one structure can be produced from the same amino acid sequence by domain swapping. We have previously shown that myoglobin (Mb) can form a domain-swapped dimer in which the hinge region is converted to a helical structure. In this study, we showed that domain-swapped dimerization of Mb was achieved by a single Ala mutation of Gly at position 80. Multiple Ala mutations at positions 81 and 82 in addition to position 80 facilitated dimerization of Mb by stabilization of the dimeric states. Domain swapping tendencies correlated well with the helical propensity of the mutated residue in a series of Mb mutants with amino acids introduced to the hinge region. These findings demonstrate that a single mutation in the hinge loop to modify helical propensity can control oligomer formation, providing new ideas to create high-order protein oligomers using domain swapping. PubMed: 32329228DOI: 10.1002/asia.202000307 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.25 Å) |
Structure validation
Download full validation report
