Fundamental Characteristics of AAA+ Protein Family Structure and Function

Joint Authors

Miller, Justin M.
Enemark, Eric J.

Source

Archaea

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

Biology

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