5M94

Crystal structure of Staphylococcus capitis divalent metal ion transporter (DMT) in complex with nanobody

Replaces:  4WGV

Summary for 5M94

• Entry DOI: 10.2210/pdb5m94/pdb
• Descriptor: Divalent metal cation transporter MntH, CAMELID ANTIBODY FRAGMENT, NANOBODY (2 entities in total)
• Functional Keywords: transition metal ion transporter, transport protein
• Biological source: Staphylococcus capitis; More
• Cellular location: Cell membrane ; Multi-pass membrane protein : A0A0S4MEX1
• Total number of polymer chains: 4
• Total formula weight: 117891.50

Authors

Dutzler, R.,Ehrnstorfer, I.A. (deposition date: 2016-10-31, release date: 2016-12-21, Last modification date: 2024-11-20)

Primary citation

Ehrnstorfer, I.A.,Geertsma, E.R.,Pardon, E.,Steyaert, J.,Dutzler, R.
Crystal structure of a SLC11 (NRAMP) transporter reveals the basis for transition-metal ion transport.
Nat. Struct. Mol. Biol., 21:990-996, 2014

PubMed Abstract: Members of the SLC11 (NRAMP) family transport iron and other transition-metal ions across cellular membranes. These membrane proteins are present in all kingdoms of life with a high degree of sequence conservation. To gain insight into the determinants of ion selectivity, we have determined the crystal structure of Staphylococcus capitis DMT (ScaDMT), a close prokaryotic homolog of the family. ScaDMT shows a familiar architecture that was previously identified in the amino acid permease LeuT. The protein adopts an inward-facing conformation with a substrate-binding site located in the center of the transporter. This site is composed of conserved residues, which coordinate Mn2+, Fe2+ and Cd2+ but not Ca2+. Mutations of interacting residues affect ion binding and transport in both ScaDMT and human DMT1. Our study thus reveals a conserved mechanism for transition-metal ion selectivity within the SLC11 family.

PubMed: 25326704
DOI: 10.1038/nsmb.2904

Experimental method

X-RAY DIFFRACTION (3.101 Å)