Energetic selection of topology in ferredoxins.

Models of early protein evolution posit the existence of short peptides that bound metals and ions and served as transporters, membranes or catalysts. The Cys-X-X-Cys-X-X-Cys heptapeptide located within bacterial ferredoxins, enclosing an Fe₄S₄ metal center, is an attractive candidate for such an ea...

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Auteurs principaux:	J Dongun Kim, Agustina Rodriguez-Granillo, David A Case, Vikas Nanda, Paul G Falkowski
Format:	article
Langue:	EN
Publié:	Public Library of Science (PLoS) 2012
Sujets:	Biology (General) QH301-705.5
Accès en ligne:	https://doaj.org/article/69e72c51036142f08f206312caf8686d
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spelling	oai:doaj.org-article:69e72c51036142f08f206312caf8686d2021-11-18T05:51:26ZEnergetic selection of topology in ferredoxins.1553-734X1553-735810.1371/journal.pcbi.1002463https://doaj.org/article/69e72c51036142f08f206312caf8686d2012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22496635/?tool=EBIhttps://doaj.org/toc/1553-734Xhttps://doaj.org/toc/1553-7358Models of early protein evolution posit the existence of short peptides that bound metals and ions and served as transporters, membranes or catalysts. The Cys-X-X-Cys-X-X-Cys heptapeptide located within bacterial ferredoxins, enclosing an Fe₄S₄ metal center, is an attractive candidate for such an early peptide. Ferredoxins are ancient proteins and the simple α+β fold is found alone or as a domain in larger proteins throughout all three kingdoms of life. Previous analyses of the heptapeptide conformation in experimentally determined ferredoxin structures revealed a pervasive right-handed topology, despite the fact that the Fe₄S₄ cluster is achiral. Conformational enumeration of a model CGGCGGC heptapeptide bound to a cubane iron-sulfur cluster indicates both left-handed and right-handed folds could exist and have comparable stabilities. However, only the natural ferredoxin topology provides a significant network of backbone-to-cluster hydrogen bonds that would stabilize the metal-peptide complex. The optimal peptide configuration (alternating α(L),α(R)) is that of an α-sheet, providing an additional mechanism where oligomerization could stabilize the peptide and facilitate iron-sulfur cluster binding.J Dongun KimAgustina Rodriguez-GranilloDavid A CaseVikas NandaPaul G FalkowskiPublic Library of Science (PLoS)articleBiology (General)QH301-705.5ENPLoS Computational Biology, Vol 8, Iss 4, p e1002463 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Biology (General) QH301-705.5
spellingShingle	Biology (General) QH301-705.5 J Dongun Kim Agustina Rodriguez-Granillo David A Case Vikas Nanda Paul G Falkowski Energetic selection of topology in ferredoxins.
description	Models of early protein evolution posit the existence of short peptides that bound metals and ions and served as transporters, membranes or catalysts. The Cys-X-X-Cys-X-X-Cys heptapeptide located within bacterial ferredoxins, enclosing an Fe₄S₄ metal center, is an attractive candidate for such an early peptide. Ferredoxins are ancient proteins and the simple α+β fold is found alone or as a domain in larger proteins throughout all three kingdoms of life. Previous analyses of the heptapeptide conformation in experimentally determined ferredoxin structures revealed a pervasive right-handed topology, despite the fact that the Fe₄S₄ cluster is achiral. Conformational enumeration of a model CGGCGGC heptapeptide bound to a cubane iron-sulfur cluster indicates both left-handed and right-handed folds could exist and have comparable stabilities. However, only the natural ferredoxin topology provides a significant network of backbone-to-cluster hydrogen bonds that would stabilize the metal-peptide complex. The optimal peptide configuration (alternating α(L),α(R)) is that of an α-sheet, providing an additional mechanism where oligomerization could stabilize the peptide and facilitate iron-sulfur cluster binding.
format	article
author	J Dongun Kim Agustina Rodriguez-Granillo David A Case Vikas Nanda Paul G Falkowski
author_facet	J Dongun Kim Agustina Rodriguez-Granillo David A Case Vikas Nanda Paul G Falkowski
author_sort	J Dongun Kim
title	Energetic selection of topology in ferredoxins.
title_short	Energetic selection of topology in ferredoxins.
title_full	Energetic selection of topology in ferredoxins.
title_fullStr	Energetic selection of topology in ferredoxins.
title_full_unstemmed	Energetic selection of topology in ferredoxins.
title_sort	energetic selection of topology in ferredoxins.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/69e72c51036142f08f206312caf8686d
work_keys_str_mv	AT jdongunkim energeticselectionoftopologyinferredoxins AT agustinarodriguezgranillo energeticselectionoftopologyinferredoxins AT davidacase energeticselectionoftopologyinferredoxins AT vikasnanda energeticselectionoftopologyinferredoxins AT paulgfalkowski energeticselectionoftopologyinferredoxins
_version_	1718424732056944640

Energetic selection of topology in ferredoxins.

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