Functional determinants of protein assembly into homomeric complexes

Abstract Approximately half of proteins with experimentally determined structures can interact with other copies of themselves and assemble into homomeric complexes, the overwhelming majority of which (>96%) are symmetric. Although homomerisation is often assumed to a functionally beneficial resu...

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Autores principales:	L. Therese Bergendahl, Joseph A. Marsh
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/510c31fdc38242a0beda3f1f7032637d
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spelling	oai:doaj.org-article:510c31fdc38242a0beda3f1f7032637d2021-12-02T16:08:09ZFunctional determinants of protein assembly into homomeric complexes10.1038/s41598-017-05084-82045-2322https://doaj.org/article/510c31fdc38242a0beda3f1f7032637d2017-07-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-05084-8https://doaj.org/toc/2045-2322Abstract Approximately half of proteins with experimentally determined structures can interact with other copies of themselves and assemble into homomeric complexes, the overwhelming majority of which (>96%) are symmetric. Although homomerisation is often assumed to a functionally beneficial result of evolutionary selection, there has been little systematic analysis of the relationship between homomer structure and function. Here, utilizing the large numbers of structures and functional annotations now available, we have investigated how proteins that assemble into different types of homomers are associated with different biological functions. We observe that homomers from different symmetry groups are significantly enriched in distinct functions, and can often provide simple physical and geometrical explanations for these associations in regards to substrate recognition or physical environment. One of the strongest associations is the tendency for metabolic enzymes to form dihedral complexes, which we suggest is closely related to allosteric regulation. We provide a physical explanation for why allostery is related to dihedral complexes: it allows for efficient propagation of conformational changes across isologous (i.e. symmetric) interfaces. Overall we demonstrate a clear relationship between protein function and homomer symmetry that has important implications for understanding protein evolution, as well as for predicting protein function and quaternary structure.L. Therese BergendahlJoseph A. MarshNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-10 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q L. Therese Bergendahl Joseph A. Marsh Functional determinants of protein assembly into homomeric complexes
description	Abstract Approximately half of proteins with experimentally determined structures can interact with other copies of themselves and assemble into homomeric complexes, the overwhelming majority of which (>96%) are symmetric. Although homomerisation is often assumed to a functionally beneficial result of evolutionary selection, there has been little systematic analysis of the relationship between homomer structure and function. Here, utilizing the large numbers of structures and functional annotations now available, we have investigated how proteins that assemble into different types of homomers are associated with different biological functions. We observe that homomers from different symmetry groups are significantly enriched in distinct functions, and can often provide simple physical and geometrical explanations for these associations in regards to substrate recognition or physical environment. One of the strongest associations is the tendency for metabolic enzymes to form dihedral complexes, which we suggest is closely related to allosteric regulation. We provide a physical explanation for why allostery is related to dihedral complexes: it allows for efficient propagation of conformational changes across isologous (i.e. symmetric) interfaces. Overall we demonstrate a clear relationship between protein function and homomer symmetry that has important implications for understanding protein evolution, as well as for predicting protein function and quaternary structure.
format	article
author	L. Therese Bergendahl Joseph A. Marsh
author_facet	L. Therese Bergendahl Joseph A. Marsh
author_sort	L. Therese Bergendahl
title	Functional determinants of protein assembly into homomeric complexes
title_short	Functional determinants of protein assembly into homomeric complexes
title_full	Functional determinants of protein assembly into homomeric complexes
title_fullStr	Functional determinants of protein assembly into homomeric complexes
title_full_unstemmed	Functional determinants of protein assembly into homomeric complexes
title_sort	functional determinants of protein assembly into homomeric complexes
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/510c31fdc38242a0beda3f1f7032637d
work_keys_str_mv	AT ltheresebergendahl functionaldeterminantsofproteinassemblyintohomomericcomplexes AT josephamarsh functionaldeterminantsofproteinassemblyintohomomericcomplexes
_version_	1718384593596317696

Functional determinants of protein assembly into homomeric complexes

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