Dephosphorylation and ion binding in prokaryotic calcium transport.

ABSTRACT: Calcium (Ca²⁺) signaling is fundamental to cellular processes in both eukaryotic and prokaryotic organisms. While the mechanisms underlying eukaryotic Ca²⁺ transport are well documented, an understanding of prokaryotic transport remains nascent. LMCA1, a Ca²⁺ adenosine triphosphatase (ATPase) from Listeria monocytogenes, has emerged as a prototype for elucidating structure and dynamics in prokaryotic Ca²⁺ 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 Ca²⁺-bound E1 state showed ion coordination by Asp⁷²⁰, Asn⁷¹⁶, and Glu²⁹². Time-resolved x-ray sol

SUBMITTER: Prabudiansyah I 

PROVIDER: S-EPMC11468904 | biostudies-literature | 2024 Oct

REPOSITORIES: biostudies-literature