5M95

STAPHYLOCOCCUS CAPITIS DIVALENT METAL ION TRANSPORTER (DMT) IN COMPLEX WITH MANGANESE

Replaces:  4WGW

Summary for 5M95

• Entry DOI: 10.2210/pdb5m95/pdb
• Related: 4WGV
• Descriptor: Divalent metal cation transporter MntH, CAMELID ANTIBODY FRAGMENT, NANOBODY, MANGANESE (II) ION (3 entities in total)
• Functional Keywords: membrane protein, transporter, slc11, transition metal ions, transport protein, nramp, dmt, leut fold
• Biological source: Staphylococcus capitis; More
• Total number of polymer chains: 4
• Total formula weight: 118207.54

Authors

Ehrnstorfer, I.A.,Geertsma, E.R.,Pardon, E.,Steyaert, J.,Dutzler, R. (deposition date: 2016-10-31, release date: 2016-11-30, Last modification date: 2024-10-16)

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-, 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 (3.4 Å)