A new structural arrangement in proteins involving lysine NH3 + group and carbonyl
Abstract Screening of the Protein Data Bank led to identification of a recurring structural motif where lysine NH3 + group interacts with backbone carbonyl. This interaction is characterized by linear atom arrangement, with carbonyl O atom positioned on the three-fold symmetry axis of the NH3 + grou...
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2017
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oai:doaj.org-article:b03b52b537194b319fa791b26d34bbf82021-12-02T15:05:42ZA new structural arrangement in proteins involving lysine NH3 + group and carbonyl10.1038/s41598-017-16584-y2045-2322https://doaj.org/article/b03b52b537194b319fa791b26d34bbf82017-11-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-16584-yhttps://doaj.org/toc/2045-2322Abstract Screening of the Protein Data Bank led to identification of a recurring structural motif where lysine NH3 + group interacts with backbone carbonyl. This interaction is characterized by linear atom arrangement, with carbonyl O atom positioned on the three-fold symmetry axis of the NH3 + group (angle Cε-Nζ-O close to 180°, distance Nζ-O ca. 2.7-3.0 Å). Typically, this linear arrangement coexists with three regular hydrogen bonds formed by lysine NH3 + group (angle Cε-Nζ-acceptor atom close to 109°, distance Nζ-acceptor atom ca. 2.7-3.0 Å). Our DFT calculations using polarizable continuum environment suggest that this newly identified linear interaction makes an appreciable contribution to protein’s energy balance, up to 2 kcal/mol. In the context of protein structure, linear interactions play a role in capping the C-termini of α-helices and 310-helices. Of note, linear interaction involving conserved lysine is consistently found in the P-loop of numerous NTPase domains, where it stabilizes the substrate-binding conformation of the P-loop. Linear interaction NH3 + – carbonyl represents an interesting example of ion-dipole interactions that has so far received little attention compared to ion-ion interactions (salt bridges) and dipole-dipole interactions (hydrogen bonds), but nevertheless represents a distinctive element of protein architecture.Olga N. RogachevaSergei A. IzmailovLyudmila V. SlipchenkoNikolai R. SkrynnikovNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-8 (2017) |
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Medicine R Science Q Olga N. Rogacheva Sergei A. Izmailov Lyudmila V. Slipchenko Nikolai R. Skrynnikov A new structural arrangement in proteins involving lysine NH3 + group and carbonyl |
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Abstract Screening of the Protein Data Bank led to identification of a recurring structural motif where lysine NH3 + group interacts with backbone carbonyl. This interaction is characterized by linear atom arrangement, with carbonyl O atom positioned on the three-fold symmetry axis of the NH3 + group (angle Cε-Nζ-O close to 180°, distance Nζ-O ca. 2.7-3.0 Å). Typically, this linear arrangement coexists with three regular hydrogen bonds formed by lysine NH3 + group (angle Cε-Nζ-acceptor atom close to 109°, distance Nζ-acceptor atom ca. 2.7-3.0 Å). Our DFT calculations using polarizable continuum environment suggest that this newly identified linear interaction makes an appreciable contribution to protein’s energy balance, up to 2 kcal/mol. In the context of protein structure, linear interactions play a role in capping the C-termini of α-helices and 310-helices. Of note, linear interaction involving conserved lysine is consistently found in the P-loop of numerous NTPase domains, where it stabilizes the substrate-binding conformation of the P-loop. Linear interaction NH3 + – carbonyl represents an interesting example of ion-dipole interactions that has so far received little attention compared to ion-ion interactions (salt bridges) and dipole-dipole interactions (hydrogen bonds), but nevertheless represents a distinctive element of protein architecture. |
format |
article |
author |
Olga N. Rogacheva Sergei A. Izmailov Lyudmila V. Slipchenko Nikolai R. Skrynnikov |
author_facet |
Olga N. Rogacheva Sergei A. Izmailov Lyudmila V. Slipchenko Nikolai R. Skrynnikov |
author_sort |
Olga N. Rogacheva |
title |
A new structural arrangement in proteins involving lysine NH3 + group and carbonyl |
title_short |
A new structural arrangement in proteins involving lysine NH3 + group and carbonyl |
title_full |
A new structural arrangement in proteins involving lysine NH3 + group and carbonyl |
title_fullStr |
A new structural arrangement in proteins involving lysine NH3 + group and carbonyl |
title_full_unstemmed |
A new structural arrangement in proteins involving lysine NH3 + group and carbonyl |
title_sort |
new structural arrangement in proteins involving lysine nh3 + group and carbonyl |
publisher |
Nature Portfolio |
publishDate |
2017 |
url |
https://doaj.org/article/b03b52b537194b319fa791b26d34bbf8 |
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