Pore‐Bound Water at the Key Residue Histidine 37 in Influenza A M2

Atomic details of structured water molecules are indispensable to understand the thermodynamics of important biological processes including the proton conduction mechanism of the M2 protein. Despite the expectation of structured water molecules based on crystal structures of Influenza A M2, only two...

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Autores principales: Movellan, Kumar Tekwani, Dervişoğlu, Rıza, Becker, Stefan, Andreas, Loren B.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8597138/
https://www.ncbi.nlm.nih.gov/pubmed/34477305
http://dx.doi.org/10.1002/anie.202103955
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author Movellan, Kumar Tekwani
Dervişoğlu, Rıza
Becker, Stefan
Andreas, Loren B.
author_facet Movellan, Kumar Tekwani
Dervişoğlu, Rıza
Becker, Stefan
Andreas, Loren B.
author_sort Movellan, Kumar Tekwani
collection PubMed
description Atomic details of structured water molecules are indispensable to understand the thermodynamics of important biological processes including the proton conduction mechanism of the M2 protein. Despite the expectation of structured water molecules based on crystal structures of Influenza A M2, only two water populations have been observed by NMR in reconstituted lipid bilayer samples. These are the bulk‐ and lipid‐associated water populations typically seen in membrane samples. Here, we detect a bound water molecule at a chemical shift of 11 ppm, located near the functional histidine 37 residue in the M2 conductance domain, which comprises residues 18 to 60. Combining 100 kHz magic‐angle spinning NMR, dynamic nuclear polarization and density functional theory calculations, we show that the bound water forms a hydrogen bond to the δ1 nitrogen of histidine 37.
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spelling pubmed-85971382021-11-22 Pore‐Bound Water at the Key Residue Histidine 37 in Influenza A M2 Movellan, Kumar Tekwani Dervişoğlu, Rıza Becker, Stefan Andreas, Loren B. Angew Chem Int Ed Engl Communications Atomic details of structured water molecules are indispensable to understand the thermodynamics of important biological processes including the proton conduction mechanism of the M2 protein. Despite the expectation of structured water molecules based on crystal structures of Influenza A M2, only two water populations have been observed by NMR in reconstituted lipid bilayer samples. These are the bulk‐ and lipid‐associated water populations typically seen in membrane samples. Here, we detect a bound water molecule at a chemical shift of 11 ppm, located near the functional histidine 37 residue in the M2 conductance domain, which comprises residues 18 to 60. Combining 100 kHz magic‐angle spinning NMR, dynamic nuclear polarization and density functional theory calculations, we show that the bound water forms a hydrogen bond to the δ1 nitrogen of histidine 37. John Wiley and Sons Inc. 2021-10-06 2021-11-02 /pmc/articles/PMC8597138/ /pubmed/34477305 http://dx.doi.org/10.1002/anie.202103955 Text en © 2021 The Authors. Angewandte Chemie International Edition published by Wiley-VCH GmbH https://creativecommons.org/licenses/by-nc/4.0/This is an open access article under the terms of the http://creativecommons.org/licenses/by-nc/4.0/ (https://creativecommons.org/licenses/by-nc/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited and is not used for commercial purposes.
spellingShingle Communications
Movellan, Kumar Tekwani
Dervişoğlu, Rıza
Becker, Stefan
Andreas, Loren B.
Pore‐Bound Water at the Key Residue Histidine 37 in Influenza A M2
title Pore‐Bound Water at the Key Residue Histidine 37 in Influenza A M2
title_full Pore‐Bound Water at the Key Residue Histidine 37 in Influenza A M2
title_fullStr Pore‐Bound Water at the Key Residue Histidine 37 in Influenza A M2
title_full_unstemmed Pore‐Bound Water at the Key Residue Histidine 37 in Influenza A M2
title_short Pore‐Bound Water at the Key Residue Histidine 37 in Influenza A M2
title_sort pore‐bound water at the key residue histidine 37 in influenza a m2
topic Communications
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8597138/
https://www.ncbi.nlm.nih.gov/pubmed/34477305
http://dx.doi.org/10.1002/anie.202103955
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