6G55

MamM CTD C267S

6G55 の概要

• エントリーDOI: 10.2210/pdb6g55/pdb
• 分子名称: Magnetosome protein MamM, SULFATE ION, BICARBONATE ION, ... (4 entities in total)
• 機能のキーワード: cation diffusion facilitator, magnetotactic bacteria, metal transport
• 由来する生物種: Magnetospirillum gryphiswaldense
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 24041.81

構造登録者

Barber-Zucker, S.,Zarivach, R. (登録日: 2018-03-29, 公開日: 2018-10-31, 最終更新日: 2024-01-17)

主引用文献

Barber-Zucker, S.,Hall, J.,Mangapuram, S.V.,Kass, I.,Kolusheva, S.,MacMillan, F.,Zarivach, R.,Henn, A.
Metal binding to the dynamic cytoplasmic domain of the cation diffusion facilitator (CDF) protein MamM induces a 'locked-in' configuration.
Febs J., 286:2193-2215, 2019

PubMed Abstract: Cation diffusion facilitator (CDF) proteins are a conserved family of transmembrane transporters that ensure cellular homeostasis of divalent transition metal cations. Metal cations bind to CDF protein's cytoplasmic C-terminal domain (CTD), leading to closure from its apo open V-shaped dimer to a tighter packed structure, followed by a conformational change of the transmembrane domain, thus enabling transport of the metal cation. By implementing a comprehensive range of biochemical and biophysical methods, we studied the molecular mechanism of metal binding to the magnetotactic bacterial CDF protein MamM CTD. Our results reveal that the CTD is rather dynamic in its apo form, and that two dependent metal-binding sites, a single central binding site and two symmetrical, peripheral sites, are available for metal binding. However, only cation binding to the peripheral sites leads to conformational changes that lock the protein in a compact state. Thus, this work reveals how metal binding is regulating the sequential uptakes of metal cations by MamM, and extends our understanding of the complex regulation mechanism of CDF proteins. DATABASE: Structural data are available in RCSB Protein Data Bank under the accession numbers: 6G64, 6G55, 6G5E and 6G6I (for CS, C267S, CS-C267S and W247A, respectively).

PubMed: 30811856
DOI: 10.1111/febs.14795

実験手法

X-RAY DIFFRACTION (1.65 Å)