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Descripción
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| A critical step in the maturation of Rhizobium leguminosarum NiFe hydrogenase involves the Ni-dependent proteolytic processing of large subunit (LSU) precursor (pre-HupL) by a specific endoprotease (HupD). A structural model for pre-HupL has been built through computational modelling and Molecular Dynamics (MD). In this model, the C-terminal tail of pre-HupL behaves as an Intrinsically Disordered Region (IDR), a type of structure known to facilitate the interaction with other proteins such as proteases. MD simulations show that a highly-stable form of pre-HupL contains a nickel atom linked to two glutamate residues located at the Terminal region and the C-terminal disordered segment of HupL (E27 and E589). Phenotypic analysis of mutants affected in each of these residues showed that both are relevant for Ni-dependent processing of pre-HupL. A stronger phenotype was associated to E27Q mutation, in line with previous work indicating that an equivalent residue would be involved in the translocation of protons in Desulfovibrio hydrogenase. Our results, along with structural modelling studies of the HupL-HupD interaction, suggest that both E27 and E589 could participate in a transient binding site for the initial incorporation of nickel into the enzyme, thus allowing efficient interaction of pre-HupL with the endoprotease. Recent studies showed that Thermococcus kodakarensis HypA interacts with LSU C- and N-terminal domains for the incorporation of nickel. | |
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Internacional
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Si |
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Nombre congreso
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Internacional Conference on Hydrogenases |
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Tipo de participación
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960 |
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Lugar del congreso
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Lisboa |
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Revisores
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Si |
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ISBN o ISSN
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0000000000 |
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DOI
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Fecha inicio congreso
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31/03/2019 |
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Fecha fin congreso
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04/04/2019 |
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Desde la página
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24 |
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Hasta la página
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25 |
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Título de las actas
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ICH2019 Book of Abstracts |