3E7K

Crystal Structure of an antiparallel coiled-coil tetramerization domain from TRPM7 channels

Summary for 3E7K

• Entry DOI: 10.2210/pdb3e7k/pdb
• Descriptor: TRPM7 channel (2 entities in total)
• Functional Keywords: coiled-coil, antiparallel, ion channel, assembly domain, trpm channel, trpm7, membrane protein
• Biological source: Rattus norvegicus (rat)
• Total number of polymer chains: 8
• Total formula weight: 50032.74

Authors

Fujiwara, Y.,Minor, D.L. (deposition date: 2008-08-18, release date: 2008-09-23, Last modification date: 2024-02-21)

Primary citation

Fujiwara, Y.,Minor, D.L.
X-ray crystal structure of a TRPM assembly domain reveals an antiparallel four-stranded coiled-coil.
J.Mol.Biol., 383:854-870, 2008

PubMed Abstract: Transient receptor potential (TRP) channels comprise a large family of tetrameric cation-selective ion channels that respond to diverse forms of sensory input. Earlier studies showed that members of the TRPM subclass possess a self-assembling tetrameric C-terminal cytoplasmic coiled-coil domain that underlies channel assembly and trafficking. Here, we present the high-resolution crystal structure of the coiled-coil domain of the channel enzyme TRPM7. The crystal structure, together with biochemical experiments, reveals an unexpected four-stranded antiparallel coiled-coil architecture that bears unique features relative to other antiparallel coiled-coils. Structural analysis indicates that a limited set of interactions encode assembly specificity determinants and uncovers a previously unnoticed segregation of TRPM assembly domains into two families that correspond with the phylogenetic divisions seen for the complete subunits. Together, the data provide a framework for understanding the mechanism of TRPM channel assembly and highlight the diversity of forms found in the coiled-coil fold.

PubMed: 18782578
DOI: 10.1016/j.jmb.2008.08.059

Experimental method

X-RAY DIFFRACTION (2.01 Å)