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Crystal structures of adenylylated and unadenylylated P(II) protein GlnK from Corynebacterium glutamicum

P(II) proteins are ubiquitous signaling proteins that are involved in the regulation of the nitrogen/carbon balance in bacteria, archaea, and some plants and algae. Signal transduction via P(II) proteins is modulated by effector molecules and post-translational modifications in the P(II) T-loop. Whe...

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Autores principales: Grau, Florian C., Burkovski, Andreas, Muller, Yves A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Union of Crystallography 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7919409/
https://www.ncbi.nlm.nih.gov/pubmed/33645536
http://dx.doi.org/10.1107/S2059798321000735
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author Grau, Florian C.
Burkovski, Andreas
Muller, Yves A.
author_facet Grau, Florian C.
Burkovski, Andreas
Muller, Yves A.
author_sort Grau, Florian C.
collection PubMed
description P(II) proteins are ubiquitous signaling proteins that are involved in the regulation of the nitrogen/carbon balance in bacteria, archaea, and some plants and algae. Signal transduction via P(II) proteins is modulated by effector molecules and post-translational modifications in the P(II) T-loop. Whereas the binding of ADP, ATP and the concomitant binding of ATP and 2-oxoglutarate (2OG) engender two distinct conformations of the T-loop that either favor or disfavor the interaction with partner proteins, the structural consequences of post-translational modifications such as phosphorylation, uridylylation and adenylylation are far less well understood. In the present study, crystal structures of the P(II) protein GlnK from Corynebacterium glutamicum have been determined, namely of adenylylated GlnK (adGlnK) and unmodified unadenylylated GlnK (unGlnK). AdGlnK has been proposed to act as an inducer of the transcription repressor AmtR, and the adenylylation of Tyr51 in GlnK has been proposed to be a prerequisite for this function. The structures of unGlnK and adGlnK allow the first atomic insights into the structural implications of the covalent attachment of an AMP moiety to the T-loop. The overall GlnK fold remains unaltered upon adenylylation, and T-loop adenylylation does not appear to interfere with the formation of the two major functionally important T-loop conformations, namely the extended T-loop in the canonical ADP-bound state and the compacted T-loop that is adopted upon the simultaneous binding of Mg-ATP and 2OG. Thus, the P(II)-typical conformational switching mechanism appears to be preserved in GlnK from C. glutamicum, while at the same time the functional repertoire becomes expanded through the accommodation of a peculiar post-translational modification.
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spelling pubmed-79194092021-03-10 Crystal structures of adenylylated and unadenylylated P(II) protein GlnK from Corynebacterium glutamicum Grau, Florian C. Burkovski, Andreas Muller, Yves A. Acta Crystallogr D Struct Biol Research Papers P(II) proteins are ubiquitous signaling proteins that are involved in the regulation of the nitrogen/carbon balance in bacteria, archaea, and some plants and algae. Signal transduction via P(II) proteins is modulated by effector molecules and post-translational modifications in the P(II) T-loop. Whereas the binding of ADP, ATP and the concomitant binding of ATP and 2-oxoglutarate (2OG) engender two distinct conformations of the T-loop that either favor or disfavor the interaction with partner proteins, the structural consequences of post-translational modifications such as phosphorylation, uridylylation and adenylylation are far less well understood. In the present study, crystal structures of the P(II) protein GlnK from Corynebacterium glutamicum have been determined, namely of adenylylated GlnK (adGlnK) and unmodified unadenylylated GlnK (unGlnK). AdGlnK has been proposed to act as an inducer of the transcription repressor AmtR, and the adenylylation of Tyr51 in GlnK has been proposed to be a prerequisite for this function. The structures of unGlnK and adGlnK allow the first atomic insights into the structural implications of the covalent attachment of an AMP moiety to the T-loop. The overall GlnK fold remains unaltered upon adenylylation, and T-loop adenylylation does not appear to interfere with the formation of the two major functionally important T-loop conformations, namely the extended T-loop in the canonical ADP-bound state and the compacted T-loop that is adopted upon the simultaneous binding of Mg-ATP and 2OG. Thus, the P(II)-typical conformational switching mechanism appears to be preserved in GlnK from C. glutamicum, while at the same time the functional repertoire becomes expanded through the accommodation of a peculiar post-translational modification. International Union of Crystallography 2021-02-19 /pmc/articles/PMC7919409/ /pubmed/33645536 http://dx.doi.org/10.1107/S2059798321000735 Text en © Grau et al. 2021 http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution (CC-BY) Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.http://creativecommons.org/licenses/by/4.0/
spellingShingle Research Papers
Grau, Florian C.
Burkovski, Andreas
Muller, Yves A.
Crystal structures of adenylylated and unadenylylated P(II) protein GlnK from Corynebacterium glutamicum
title Crystal structures of adenylylated and unadenylylated P(II) protein GlnK from Corynebacterium glutamicum
title_full Crystal structures of adenylylated and unadenylylated P(II) protein GlnK from Corynebacterium glutamicum
title_fullStr Crystal structures of adenylylated and unadenylylated P(II) protein GlnK from Corynebacterium glutamicum
title_full_unstemmed Crystal structures of adenylylated and unadenylylated P(II) protein GlnK from Corynebacterium glutamicum
title_short Crystal structures of adenylylated and unadenylylated P(II) protein GlnK from Corynebacterium glutamicum
title_sort crystal structures of adenylylated and unadenylylated p(ii) protein glnk from corynebacterium glutamicum
topic Research Papers
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7919409/
https://www.ncbi.nlm.nih.gov/pubmed/33645536
http://dx.doi.org/10.1107/S2059798321000735
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