In silico investigation of conformational motions in superfamily 2 helicase proteins.

Helicases are motor proteins that play a central role in the metabolism of DNA and RNA in biological cells. Using the energy of ATP molecules, they are able to translocate along the nucleic acids and unwind their duplex structure. They have been extensively characterized in the past and grouped into...

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Autores principales:	Holger Flechsig, Denny Popp, Alexander S Mikhailov
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2011
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/c307df01c7d64647a80fd6d2a4cf6676
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spelling	oai:doaj.org-article:c307df01c7d64647a80fd6d2a4cf66762021-11-18T06:49:56ZIn silico investigation of conformational motions in superfamily 2 helicase proteins.1932-620310.1371/journal.pone.0021809https://doaj.org/article/c307df01c7d64647a80fd6d2a4cf66762011-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/21829442/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203Helicases are motor proteins that play a central role in the metabolism of DNA and RNA in biological cells. Using the energy of ATP molecules, they are able to translocate along the nucleic acids and unwind their duplex structure. They have been extensively characterized in the past and grouped into superfamilies based on structural similarities and sequential motifs. However, their functional aspects and the mechanism of their operation are not yet well understood. Here, we consider three helicases from the major superfamily 2--Hef, Hel308 and XPD--and study their conformational dynamics by using coarse-grained relaxational elastic network models. Specifically, their responses to mechanical perturbations are analyzed. This enables us to identify robust and ordered conformational motions which may underlie the functional activity of these proteins. As we show, such motions are well-organized and have large amplitudes. Their possible roles in the processing of nucleic substrate are discussed.Holger FlechsigDenny PoppAlexander S MikhailovPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 6, Iss 7, p e21809 (2011)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Holger Flechsig Denny Popp Alexander S Mikhailov In silico investigation of conformational motions in superfamily 2 helicase proteins.
description	Helicases are motor proteins that play a central role in the metabolism of DNA and RNA in biological cells. Using the energy of ATP molecules, they are able to translocate along the nucleic acids and unwind their duplex structure. They have been extensively characterized in the past and grouped into superfamilies based on structural similarities and sequential motifs. However, their functional aspects and the mechanism of their operation are not yet well understood. Here, we consider three helicases from the major superfamily 2--Hef, Hel308 and XPD--and study their conformational dynamics by using coarse-grained relaxational elastic network models. Specifically, their responses to mechanical perturbations are analyzed. This enables us to identify robust and ordered conformational motions which may underlie the functional activity of these proteins. As we show, such motions are well-organized and have large amplitudes. Their possible roles in the processing of nucleic substrate are discussed.
format	article
author	Holger Flechsig Denny Popp Alexander S Mikhailov
author_facet	Holger Flechsig Denny Popp Alexander S Mikhailov
author_sort	Holger Flechsig
title	In silico investigation of conformational motions in superfamily 2 helicase proteins.
title_short	In silico investigation of conformational motions in superfamily 2 helicase proteins.
title_full	In silico investigation of conformational motions in superfamily 2 helicase proteins.
title_fullStr	In silico investigation of conformational motions in superfamily 2 helicase proteins.
title_full_unstemmed	In silico investigation of conformational motions in superfamily 2 helicase proteins.
title_sort	in silico investigation of conformational motions in superfamily 2 helicase proteins.
publisher	Public Library of Science (PLoS)
publishDate	2011
url	https://doaj.org/article/c307df01c7d64647a80fd6d2a4cf6676
work_keys_str_mv	AT holgerflechsig insilicoinvestigationofconformationalmotionsinsuperfamily2helicaseproteins AT dennypopp insilicoinvestigationofconformationalmotionsinsuperfamily2helicaseproteins AT alexandersmikhailov insilicoinvestigationofconformationalmotionsinsuperfamily2helicaseproteins
_version_	1718424377704316928

In silico investigation of conformational motions in superfamily 2 helicase proteins.

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