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PMID:25326704

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Citation

Ehrnstorfer, IA, Geertsma, ER, Pardon, E, Steyaert, J and Dutzler, R (2014) Crystal structure of a SLC11 (NRAMP) transporter reveals the basis for transition-metal ion transport. Nat. Struct. Mol. Biol. 21:990-6

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.

Links

PubMed Online version:10.1038/nsmb.2904

Keywords

Amino Acid Sequence; Amino Acid Transport Systems/chemistry; Amino Acid Transport Systems/genetics; Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Binding Sites; Cadmium/chemistry; Cation Transport Proteins/chemistry; Cation Transport Proteins/genetics; Cations, Divalent; Conserved Sequence; Crystallography, X-Ray; Escherichia coli/genetics; Escherichia coli/metabolism; Gene Expression; Humans; Ion Transport; Iron/chemistry; Manganese/chemistry; Models, Molecular; Molecular Sequence Data; Protein Binding; Protein Conformation; Recombinant Proteins; Staphylococcus/chemistry; Staphylococcus/metabolism; Structural Homology, Protein; Substrate Specificity; Transcription Factors/chemistry; Transcription Factors/genetics

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

HUMAN:NRAM2

located_in

GO:0005887: integral component of plasma membrane

ECO:0000315: mutant phenotype evidence used in manual assertion

C

Seeded From UniProt

complete

HUMAN:NRAM2

involved_in

GO:0070574: cadmium ion transmembrane transport

ECO:0000314: direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

HUMAN:NRAM2

part_of

GO:0005887: integral component of plasma membrane

ECO:0000315: mutant phenotype evidence used in manual assertion

C

Seeded From UniProt

complete

HUMAN:NRAM2

enables

GO:0046915: transition metal ion transmembrane transporter activity

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

HUMAN:NRAM2

enables

GO:0046870: cadmium ion binding

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

HUMAN:Q8IUD7

enables

GO:0046870: cadmium ion binding

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

HUMAN:Q8IUD7

enables

GO:0046915: transition metal ion transmembrane transporter activity

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

HUMAN:Q8IUD7

part_of

GO:0005887: integral component of plasma membrane

ECO:0000315: mutant phenotype evidence used in manual assertion

C

Seeded From UniProt

complete

HUMAN:Q8IUD7

involved_in

GO:0070574: cadmium ion transmembrane transport

ECO:0000314: direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

Notes

See also

References

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