4WGV: Crystal Structure Of Staphylococcus Capitis Divalent Metal Ion Transporter (dmt) In Complex With Nanobody

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.
PDB ID: 4WGVDownload
MMDB ID: 124227
PDB Deposition Date: 2014/9/19
Updated in MMDB: 2014/12
Experimental Method:
x-ray diffraction
Resolution: 3.1  Å
Source Organism:
Staphylococcus capitis VCU116
Similar Structures:
Biological Unit for 4WGV: tetrameric; determined by software (PISA)
Molecular Components in 4WGV
Label Count Molecule
Proteins (4 molecules)
Divalent Metal Cation Transporter Mnth
Molecule annotation
Camelid Antibody Fragment, Nanobody
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB