Coordination promiscuity guarantees metal substrate selection in transmembrane primary-active Zn2+ pumps

Marc J. Gallenito; Gordon W. Irvine; Limei Zhang; Gabriele Meloni

doi:10.1039/c9cc05936a

Coordination promiscuity guarantees metal substrate selection in transmembrane primary-active Zn²⁺ pumps

Marc J. Gallenito, Gordon W. Irvine, Limei Zhang, Gabriele Meloni

Research output: Contribution to journal › Article › peer-review

2 Scopus citations

Abstract

Metal selectivity in P_1B-type ATPase pumps appears to be determined by amino acid motifs on their transmembrane helices. We reveal the principles governing substrate promiscuity towards first-, second- and third-row transition metals in a transmembrane Zn²⁺/Cd²⁺/Hg²⁺/Pb²⁺ P-type ATPase (ZntA), by dissecting its coordination chemistry. Atomic resolution characterization in detergent micelles and lipid bilayers reveals a "plastic" transmembrane metal-binding site that selects substrates by unique and diverse, yet defined, coordination geometries and ligand-metal distances.

Original language	English (US)
Pages (from-to)	10844-10847
Number of pages	4
Journal	Chemical Communications
Volume	55
Issue number	73
DOIs	https://doi.org/10.1039/c9cc05936a
State	Published - 2019

ASJC Scopus subject areas

Catalysis
Electronic, Optical and Magnetic Materials
Ceramics and Composites
Chemistry(all)
Surfaces, Coatings and Films
Metals and Alloys
Materials Chemistry

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10.1039/c9cc05936a

Cite this

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title = "Coordination promiscuity guarantees metal substrate selection in transmembrane primary-active Zn2+ pumps",

abstract = "Metal selectivity in P1B-type ATPase pumps appears to be determined by amino acid motifs on their transmembrane helices. We reveal the principles governing substrate promiscuity towards first-, second- and third-row transition metals in a transmembrane Zn2+/Cd2+/Hg2+/Pb2+ P-type ATPase (ZntA), by dissecting its coordination chemistry. Atomic resolution characterization in detergent micelles and lipid bilayers reveals a {"}plastic{"} transmembrane metal-binding site that selects substrates by unique and diverse, yet defined, coordination geometries and ligand-metal distances.",

author = "Gallenito, {Marc J.} and Irvine, {Gordon W.} and Limei Zhang and Gabriele Meloni",

note = "Funding Information: The work was supported by the Robert A. Welch Foundation (AT-1935-20170325 to G. M.), the National Institute Of General Medical Sciences (NIH, R35GM128704 to G. M.), a Marie Curie Fellowship (252961 to G. M.), and P30 GM103335 to L. Z. through the Nebraska Redox Biology Center. Publisher Copyright: This journal is {\textcopyright} 2019 The Royal Society of Chemistry.",

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doi = "10.1039/c9cc05936a",

language = "English (US)",

volume = "55",

pages = "10844--10847",

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T1 - Coordination promiscuity guarantees metal substrate selection in transmembrane primary-active Zn2+ pumps

AU - Gallenito, Marc J.

AU - Irvine, Gordon W.

AU - Zhang, Limei

AU - Meloni, Gabriele

N1 - Funding Information: The work was supported by the Robert A. Welch Foundation (AT-1935-20170325 to G. M.), the National Institute Of General Medical Sciences (NIH, R35GM128704 to G. M.), a Marie Curie Fellowship (252961 to G. M.), and P30 GM103335 to L. Z. through the Nebraska Redox Biology Center. Publisher Copyright: This journal is © 2019 The Royal Society of Chemistry.

PY - 2019

Y1 - 2019

N2 - Metal selectivity in P1B-type ATPase pumps appears to be determined by amino acid motifs on their transmembrane helices. We reveal the principles governing substrate promiscuity towards first-, second- and third-row transition metals in a transmembrane Zn2+/Cd2+/Hg2+/Pb2+ P-type ATPase (ZntA), by dissecting its coordination chemistry. Atomic resolution characterization in detergent micelles and lipid bilayers reveals a "plastic" transmembrane metal-binding site that selects substrates by unique and diverse, yet defined, coordination geometries and ligand-metal distances.

AB - Metal selectivity in P1B-type ATPase pumps appears to be determined by amino acid motifs on their transmembrane helices. We reveal the principles governing substrate promiscuity towards first-, second- and third-row transition metals in a transmembrane Zn2+/Cd2+/Hg2+/Pb2+ P-type ATPase (ZntA), by dissecting its coordination chemistry. Atomic resolution characterization in detergent micelles and lipid bilayers reveals a "plastic" transmembrane metal-binding site that selects substrates by unique and diverse, yet defined, coordination geometries and ligand-metal distances.

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Coordination promiscuity guarantees metal substrate selection in transmembrane primary-active Zn²⁺ pumps

Abstract

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