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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...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Hindawi Publishing Corporation
2016
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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. |
format | Online Article Text |
id | pubmed-5039278 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Hindawi Publishing Corporation |
record_format | MEDLINE/PubMed |
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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