4TXI

Construct of MICAL-1 containing the monooxygenase and calponin homology domains

4TXI の概要

• エントリーDOI: 10.2210/pdb4txi/pdb
• 関連するPDBエントリー: 4TXK
• 分子名称: Protein-methionine sulfoxide oxidase MICAL1, FLAVIN-ADENINE DINUCLEOTIDE, CHLORIDE ION, ... (5 entities in total)
• 機能のキーワード: monooxygenase, calponin homology, mical, oxidoreductase
• 由来する生物種: Mus musculus (Mouse)
• 細胞内の位置: Cytoplasm : Q8VDP3
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 68525.28

構造登録者

Alqassim, S.S.,Amzel, L.M.,Bianchet, M.A. (登録日: 2014-07-03, 公開日: 2016-01-13, 最終更新日: 2023-12-27)

主引用文献

Alqassim, S.S.,Urquiza, M.,Borgnia, E.,Nagib, M.,Amzel, L.M.,Bianchet, M.A.
Modulation of MICAL Monooxygenase Activity by its Calponin Homology Domain: Structural and Mechanistic Insights.
Sci Rep, 6:22176-22176, 2016

PubMed Abstract: MICALs (Molecule Interacting with CasL) are conserved multidomain enzymes essential for cytoskeletal reorganization in nerve development, endocytosis, and apoptosis. In these enzymes, a type-2 calponin homology (CH) domain always follows an N-terminal monooxygenase (MO) domain. Although the CH domain is required for MICAL-1 cellular localization and actin-associated function, its contribution to the modulation of MICAL activity towards actin remains unclear. Here, we present the structure of a fragment of MICAL-1 containing the MO and the CH domains-determined by X-ray crystallography and small angle scattering-as well as kinetics experiments designed to probe the contribution of the CH domain to the actin-modification activity. Our results suggest that the CH domain, which is loosely connected to the MO domain by a flexible linker and is far away from the catalytic site, couples F-actin to the enhancement of redox activity of MICALMO-CH by a cooperative mechanism involving a trans interaction between adjacently bound molecules. Binding cooperativity is also observed in other proteins regulating actin assembly/disassembly dynamics, such as ADF/Cofilins.

PubMed: 26935886
DOI: 10.1038/srep22176

実験手法

X-RAY DIFFRACTION (2.309 Å)