8ONT

Structure of Setaria italica NRAT in complex with a nanobody

Summary for 8ONT

• Entry DOI: 10.2210/pdb8ont/pdb
• EMDB information: 17000
• Descriptor: NRAMP related aluminium transporter, Nanobody1, DIUNDECYL PHOSPHATIDYL CHOLINE, ... (4 entities in total)
• Functional Keywords: nrat, nramp, slc11, metal uptake, aluminium transporter, transport protein
• Biological source: Setaria italica (foxtail millet); More
• Total number of polymer chains: 2
• Total formula weight: 73841.61

Authors

Ramanadane, K.,Liziczai, M.,Markovic, D.,Straub, M.S.,Rosalen, G.T.,Udovcic, A.,Dutzler, R.,Manatschal, C. (deposition date: 2023-04-03, release date: 2023-04-12, Last modification date: 2025-07-09)

Primary citation

Ramanadane, K.,Liziczai, M.,Markovic, D.,Straub, M.S.,Rosalen, G.T.,Udovcic, A.,Dutzler, R.,Manatschal, C.
Structural and functional properties of a plant NRAMP-related aluminum transporter.
Elife, 12:-, 2023

PubMed Abstract: The transport of transition metal ions by members of the SLC11/NRAMP family constitutes a ubiquitous mechanism for the uptake of Fe and Mn across all kingdoms of life. Despite the strong conservation of the family, two of its branches have evolved a distinct substrate preference with one mediating Mg uptake in prokaryotes and another the transport of Al into plant cells. Our previous work on the SLC11 transporter from revealed the basis for its Mg selectivity (Ramanadane et al., 2022). Here, we have addressed the structural and functional properties of a putative Al transporter from . We show that the protein transports diverse divalent metal ions and binds the trivalent ions Al and Ga, which are both presumable substrates. Its cryo-electron microscopy (cryo-EM) structure displays an occluded conformation that is closer to an inward- than an outward-facing state, with a binding site that is remodeled to accommodate the increased charge density of its transported substrate.

PubMed: 37074929
DOI: 10.7554/eLife.85641

Experimental method

ELECTRON MICROSCOPY (3.66 Å)