6LTL

The dimeric structure of G80A myoglobin

6LTL の概要

• エントリーDOI: 10.2210/pdb6ltl/pdb
• 関連するPDBエントリー: 6LS8
• 分子名称: Myoglobin, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
• 機能のキーワード: oxygen storage, oxygen binding
• 由来する生物種: Equus caballus (Horse)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 35228.05

構造登録者

Nagao, S.,Suda, A.,Kobayashi, H.,Shibata, N.,Higuchi, Y.,Hirota, S. (登録日: 2020-01-22, 公開日: 2020-05-06, 最終更新日: 2023-11-29)

主引用文献

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

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: 32329228
DOI: 10.1002/asia.202000307

実験手法

X-RAY DIFFRACTION (1.25 Å)