Publikation: Heme uptake across the outer membrane as revealed by crystal structures of the receptor-hemophore complex
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2009
Autor:innen
Krieg, Stefanie
Huché, Frédéric
Izadi-Pruneyre, Nadia
Lecroisey, Anne
Wandersmann, Cécile
Delepelaire, Philippe
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PNAS. 2009, 106(4), pp. 1045-1050. ISSN 0027-8424. eISSN 1091-6490. Available under: doi: 10.1073/pnas.0809406106
Zusammenfassung
Gram-negative bacteria use specific heme uptake systems, relying on outer membrane receptors and excreted heme-binding proteins (hemophores) to scavenge and actively transport heme, To unravel the unknown molecular details involved. we present 3 structures of the Serratia marcescens receptor HasR in complex with its hemophore HasA. The transfer of heme over a distance of 9 A from its high-affinity site in HasA into a site of lower affinity in HasR is coupled with the exergonic complex formation of the 2 proteins. Upon docking to the receptor. 1 of the 2 axial heme coordinations of the hemophore is initially broken. but the position and orientation of the heme is preserved, Subsequently. steric displacement of heme by a receptor residue ruptures the other axial, coordination. leading to heme transfer into the receptor,
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Fachgebiet (DDC)
570 Biowissenschaften, Biologie
Schlagwörter
heme binding, iron uptake, membrane protein, membrane transport, protein complex
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KRIEG, Stefanie, Frédéric HUCHÉ, Kay DIEDERICHS, Nadia IZADI-PRUNEYRE, Anne LECROISEY, Cécile WANDERSMANN, Philippe DELEPELAIRE, Wolfram WELTE, 2009. Heme uptake across the outer membrane as revealed by crystal structures of the receptor-hemophore complex. In: PNAS. 2009, 106(4), pp. 1045-1050. ISSN 0027-8424. eISSN 1091-6490. Available under: doi: 10.1073/pnas.0809406106BibTex
@article{Krieg2009uptak-8026,
year={2009},
doi={10.1073/pnas.0809406106},
title={Heme uptake across the outer membrane as revealed by crystal structures of the receptor-hemophore complex},
number={4},
volume={106},
issn={0027-8424},
journal={PNAS},
pages={1045--1050},
author={Krieg, Stefanie and Huché, Frédéric and Diederichs, Kay and Izadi-Pruneyre, Nadia and Lecroisey, Anne and Wandersmann, Cécile and Delepelaire, Philippe and Welte, Wolfram}
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<dcterms:abstract xml:lang="eng">Gram-negative bacteria use specific heme uptake systems, relying on outer membrane receptors and excreted heme-binding proteins (hemophores) to scavenge and actively transport heme, To unravel the unknown molecular details involved. we present 3 structures of the Serratia marcescens receptor HasR in complex with its hemophore HasA. The transfer of heme over a distance of 9 A from its high-affinity site in HasA into a site of lower affinity in HasR is coupled with the exergonic complex formation of the 2 proteins. Upon docking to the receptor. 1 of the 2 axial heme coordinations of the hemophore is initially broken. but the position and orientation of the heme is preserved, Subsequently. steric displacement of heme by a receptor residue ruptures the other axial, coordination. leading to heme transfer into the receptor,</dcterms:abstract>
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