9EVC

CryoEM structure of LMCA1 in E1-Ca state

9EVC の概要

• エントリーDOI: 10.2210/pdb9evc/pdb
• EMDBエントリー: 19998
• 分子名称: Calcium-transporting ATPase lmo0841, CALCIUM ION (2 entities in total)
• 機能のキーワード: transporter, membrane protein
• 由来する生物種: Listeria monocytogenes
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 95735.62

構造登録者

Prabudiansyah, I.,Andersson, M. (登録日: 2024-03-28, 公開日: 2025-02-05, 最終更新日: 2025-02-19)

主引用文献

Prabudiansyah, I.,Oradd, F.,Magkakis, K.,Pounot, K.,Levantino, M.,Andersson, M.
Dephosphorylation and ion binding in prokaryotic calcium transport.
Sci Adv, 10:eadp2916-eadp2916, 2024

PubMed Abstract: Calcium (Ca) signaling is fundamental to cellular processes in both eukaryotic and prokaryotic organisms. While the mechanisms underlying eukaryotic Ca transport are well documented, an understanding of prokaryotic transport remains nascent. LMCA1, a Ca adenosine triphosphatase (ATPase) from , has emerged as a prototype for elucidating structure and dynamics in prokaryotic Ca transport. Here, we used a multidisciplinary approach integrating kinetics, structure, and dynamics to unravel the intricacies of LMCA1 function. A cryo-electron microscopy (cryo-EM) structure of a Ca-bound E1 state showed ion coordination by Asp, Asn, and Glu. Time-resolved x-ray solution scattering experiments identified phosphorylation as the rate-determining step. A cryo-EM E2P state structure exhibited remarkable similarities to a SERCA1a E2-P* state, which highlights the essential role of the unique P-A domain interface in enhancing dephosphorylation rates and reconciles earlier proposed mechanisms. Our study underscores the distinctiveness between eukaryotic and prokaryotic Ca ATPase transport systems and positions LMCA1 as a promising drug target for developing antimicrobial strategies.

PubMed: 39908574
DOI: 10.1126/sciadv.adp2916

実験手法

ELECTRON MICROSCOPY (3.73 Å)