6EEL

Crystal Structure of Myoferlin C2A with divalent cation

6EEL の概要

• エントリーDOI: 10.2210/pdb6eel/pdb
• 関連するPDBエントリー: 2DMH
• 分子名称: Myoferlin, STRONTIUM ION (3 entities in total)
• 機能のキーワード: ferlin, c2 domain, calcium-binding, metal binding protein
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 43306.99

構造登録者

Sutton, R.B.,Harsini, F.M.,Rice, A.M. (登録日: 2018-08-14, 公開日: 2019-05-22, 最終更新日: 2023-10-11)

主引用文献

Harsini, F.M.,Bui, A.A.,Rice, A.M.,Chebrolu, S.,Fuson, K.L.,Turtoi, A.,Bradberry, M.,Chapman, E.R.,Sutton, R.B.
Structural Basis for the Distinct Membrane Binding Activity of the Homologous C2A Domains of Myoferlin and Dysferlin.
J.Mol.Biol., 431:2112-2126, 2019

PubMed Abstract: Dysferlin has been implicated in acute membrane repair processes, whereas myoferlin's activity is maximal during the myoblast fusion stage of early skeletal muscle cell development. Both proteins are similar in size and domain structure; however, despite the overall similarity, myoferlin's known physiological functions do not overlap with those of dysferlin. Here we present for the first time the X-ray crystal structure of human myoferlin C2A to 1.9 Å resolution bound to two divalent cations, and compare its three-dimensional structure and membrane binding activities to that of dysferlin C2A. We find that while dysferlin C2A binds membranes in a Ca-dependent manner, Ca binding was the rate-limiting kinetic step for this interaction. Myoferlin C2A, on the other hand, binds two calcium ions with an affinity 3-fold lower than that of dysferlin C2A; and, surprisingly, myoferlin C2A binds only marginally to phospholipid mixtures with a high fraction of phosphatidylserine.

PubMed: 31004665
DOI: 10.1016/j.jmb.2019.04.006

実験手法

X-RAY DIFFRACTION (1.93 Å)