Molecular Mechanism of Nramp-Family Transition Metal Transport
Autor: | Rachelle Gaudet, Aaron T. Bozzi |
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Rok vydání: | 2021 |
Předmět: |
Ions
0303 health sciences Conformational change Metal binding Chemistry Mechanism (biology) Biological Transport Computational biology Article Transition metal transport Structure-Activity Relationship 03 medical and health sciences 0302 clinical medicine Metals Structural Biology Multigene Family Proton transport Symporter Molecular mechanism Voltage dependence Cation Transport Proteins Molecular Biology 030217 neurology & neurosurgery Protein Binding 030304 developmental biology |
Zdroj: | J Mol Biol |
ISSN: | 0022-2836 |
DOI: | 10.1016/j.jmb.2021.166991 |
Popis: | The Natural resistance-associated macrophage protein (Nramp) family of transition metal transporters enables uptake and trafficking of essential micronutrients that all organisms must acquire to survive. Two decades after Nramps were identified as proton-driven, voltage-dependent secondary transporters, multiple Nramp crystal structures have begun to illustrate the fine details of the transport process and provide a new framework for understanding a wealth of preexisting biochemical data. Here we review the relevant literature pertaining to Nramps' biological roles and especially their conserved molecular mechanism, including our updated understanding of conformational change, metal binding and transport, substrate selectivity, proton transport, proton-metal coupling, and voltage dependence. We ultimately describe how the Nramp family has adapted the LeuT fold common to many secondary transporters to provide selective transition-metal transport with a mechanism that deviates from the canonical model of symport. |
Databáze: | OpenAIRE |
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