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Fundamental Characteristics of AAA+ Protein Family Structure and Function

Many complex cellular events depend on multiprotein complexes known as molecular machines to efficiently couple the energy derived from adenosine triphosphate hydrolysis to the generation of mechanical force. Members of the AAA+ ATPase superfamily (ATPases Associated with various cellular Activities...

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Detalles Bibliográficos
Autores principales: Miller, Justin M., Enemark, Eric J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Hindawi Publishing Corporation 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5039278/
https://www.ncbi.nlm.nih.gov/pubmed/27703410
http://dx.doi.org/10.1155/2016/9294307
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author Miller, Justin M.
Enemark, Eric J.
author_facet Miller, Justin M.
Enemark, Eric J.
author_sort Miller, Justin M.
collection PubMed
description Many complex cellular events depend on multiprotein complexes known as molecular machines to efficiently couple the energy derived from adenosine triphosphate hydrolysis to the generation of mechanical force. Members of the AAA+ ATPase superfamily (ATPases Associated with various cellular Activities) are critical components of many molecular machines. AAA+ proteins are defined by conserved modules that precisely position the active site elements of two adjacent subunits to catalyze ATP hydrolysis. In many cases, AAA+ proteins form a ring structure that translocates a polymeric substrate through the central channel using specialized loops that project into the central channel. We discuss the major features of AAA+ protein structure and function with an emphasis on pivotal aspects elucidated with archaeal proteins.
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spelling pubmed-50392782016-10-04 Fundamental Characteristics of AAA+ Protein Family Structure and Function Miller, Justin M. Enemark, Eric J. Archaea Review Article Many complex cellular events depend on multiprotein complexes known as molecular machines to efficiently couple the energy derived from adenosine triphosphate hydrolysis to the generation of mechanical force. Members of the AAA+ ATPase superfamily (ATPases Associated with various cellular Activities) are critical components of many molecular machines. AAA+ proteins are defined by conserved modules that precisely position the active site elements of two adjacent subunits to catalyze ATP hydrolysis. In many cases, AAA+ proteins form a ring structure that translocates a polymeric substrate through the central channel using specialized loops that project into the central channel. We discuss the major features of AAA+ protein structure and function with an emphasis on pivotal aspects elucidated with archaeal proteins. Hindawi Publishing Corporation 2016-09-14 /pmc/articles/PMC5039278/ /pubmed/27703410 http://dx.doi.org/10.1155/2016/9294307 Text en Copyright © 2016 J. M. Miller and E. J. Enemark. https://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Review Article
Miller, Justin M.
Enemark, Eric J.
Fundamental Characteristics of AAA+ Protein Family Structure and Function
title Fundamental Characteristics of AAA+ Protein Family Structure and Function
title_full Fundamental Characteristics of AAA+ Protein Family Structure and Function
title_fullStr Fundamental Characteristics of AAA+ Protein Family Structure and Function
title_full_unstemmed Fundamental Characteristics of AAA+ Protein Family Structure and Function
title_short Fundamental Characteristics of AAA+ Protein Family Structure and Function
title_sort fundamental characteristics of aaa+ protein family structure and function
topic Review Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5039278/
https://www.ncbi.nlm.nih.gov/pubmed/27703410
http://dx.doi.org/10.1155/2016/9294307
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