Fundamental Characteristics of AAA+ Protein Family Structure and Function
Joint Authors
Miller, Justin M.
Enemark, Eric J.
Source
Issue
Vol. 2016, Issue 2016 (31 Dec. 2016), pp.1-12, 12 p.
Publisher
Hindawi Publishing Corporation
Publication Date
2016-09-14
Country of Publication
Egypt
No. of Pages
12
Main Subjects
Abstract EN
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.
American Psychological Association (APA)
Miller, Justin M.& Enemark, Eric J.. 2016. Fundamental Characteristics of AAA+ Protein Family Structure and Function. Archaea،Vol. 2016, no. 2016, pp.1-12.
https://search.emarefa.net/detail/BIM-1096660
Modern Language Association (MLA)
Miller, Justin M.& Enemark, Eric J.. Fundamental Characteristics of AAA+ Protein Family Structure and Function. Archaea No. 2016 (2016), pp.1-12.
https://search.emarefa.net/detail/BIM-1096660
American Medical Association (AMA)
Miller, Justin M.& Enemark, Eric J.. Fundamental Characteristics of AAA+ Protein Family Structure and Function. Archaea. 2016. Vol. 2016, no. 2016, pp.1-12.
https://search.emarefa.net/detail/BIM-1096660
Data Type
Journal Articles
Language
English
Notes
Includes bibliographical references
Record ID
BIM-1096660