6BV7

NMR structure of Sodium/Calcium Exchanger 1 (NCX1) Two-helix Bundle (THB) domain

Summary for 6BV7

• Entry DOI: 10.2210/pdb6bv7/pdb
• NMR Information: BMRB: 30379
• Descriptor: Sodium/calcium exchanger 1 (1 entity in total)
• Functional Keywords: two-helix bundle, membrane protein
• Biological source: Canis lupus familiaris (Dog)
• Total number of polymer chains: 1
• Total formula weight: 6788.54

Authors

Yuan, J.,Yuan, C.,Bruschweiler, R. (deposition date: 2017-12-12, release date: 2018-06-20, Last modification date: 2024-05-01)

Primary citation

Yuan, J.,Yuan, C.,Xie, M.,Yu, L.,Bruschweiler-Li, L.,Bruschweiler, R.
The Intracellular Loop of the Na+/Ca2+Exchanger Contains an "Awareness Ribbon"-Shaped Two-Helix Bundle Domain.
Biochemistry, 57:5096-5104, 2018

PubMed Abstract: The Na/Ca exchanger (NCX) is a ubiquitous single-chain membrane protein that plays a major role in regulating the intracellular Ca homeostasis by the counter transport of Na and Ca across the cell membrane. Other than its prokaryotic counterpart, which contains only the transmembrane domain and is self-sufficient as an active ion transporter, the eukaryotic NCX protein possesses in addition a large intracellular loop that senses intracellular calcium signals and controls the activation of ion transport across the membrane. This provides a necessary layer of regulation for the more complex function of eukaryotic cells. The Ca sensor in the intracellular loop is known as the Ca-binding domain (CBD12). However, how the signaling of the allosteric intracellular Ca binding propagates and results in transmembrane ion transportation still lacks a detailed explanation. Further structural and dynamics characterization of the intracellular loop flanking both sides of CBD12 is therefore imperative. Here, we report the identification and characterization of another structured domain that is N-terminal to CBD12 in the intracellular loop using solution nuclear magnetic resonance (NMR) spectroscopy. The atomistic structure of this domain reveals that two tandem long α-helices, connected by a short linker, form a stable crossover two-helix bundle (THB), resembling an "awareness ribbon". Considering the highly conserved amino acid sequence of the THB domain, the detailed structural and dynamics properties of the THB domain will be common among NCXs from different species and will contribute toward the understanding of the regulatory mechanism of eukaryotic Na/Ca exchangers.

PubMed: 29898361
DOI: 10.1021/acs.biochem.8b00300

Experimental method

SOLUTION NMR