Fundamental Characteristics of AAA+ Protein Family Structure and Function

المؤلفون المشاركون

Miller, Justin M.
Enemark, Eric J.

المصدر

Archaea

العدد

المجلد 2016، العدد 2016 (31 ديسمبر/كانون الأول 2016)، ص ص. 1-12، 12ص.

الناشر

Hindawi Publishing Corporation

تاريخ النشر

2016-09-14

دولة النشر

مصر

عدد الصفحات

12

التخصصات الرئيسية

الأحياء

الملخص 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.

نمط استشهاد جمعية علماء النفس الأمريكية (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

نمط استشهاد الجمعية الأمريكية للغات الحديثة (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

نمط استشهاد الجمعية الطبية الأمريكية (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

نوع البيانات

مقالات

لغة النص

الإنجليزية

الملاحظات

Includes bibliographical references

رقم السجل

BIM-1096660