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“谷氨酸开关”在AAA+蛋白中提供了ATP酶活性与配体结合之间的联系。

The 'glutamate switch' provides a link between ATPase activity and ligand binding in AAA+ proteins.

作者信息

Zhang Xiaodong, Wigley Dale B

机构信息

Division of Molecular Biosciences, Centre for Structural Biology, Department of Life Sciences, Faculty of Natural Sciences, Imperial College London, London SW72AZ, UK.

出版信息

Nat Struct Mol Biol. 2008 Nov;15(11):1223-7. doi: 10.1038/nsmb.1501. Epub 2008 Oct 12.

DOI:10.1038/nsmb.1501
PMID:18849995
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2806578/
Abstract

AAA+ proteins carry out diverse functions in cells. In most cases, their ATPase activity is tightly regulated by protein partners and target ligands, but the mechanism for this control has remained unclear. We have identified a conserved link between the ligand binding and ATPase sites in AAA+ proteins. This link, which we call the 'glutamate switch', regulates ATPase activity directly in response to the binding of target ligands by controlling the orientation of the conserved glutamate residue in the DExx motif, switching it between active and inactive conformations. The reasons for this level of control of the ATPase activity are discussed in the context of the biological processes catalyzed by AAA+ proteins.

摘要

AAA+蛋白在细胞中执行多种功能。在大多数情况下，它们的ATP酶活性受到蛋白质伴侣和靶配体的严格调控，但这种调控机制尚不清楚。我们已经在AAA+蛋白中确定了配体结合位点和ATP酶位点之间的保守联系。我们将这种联系称为“谷氨酸开关”，它通过控制DExx基序中保守谷氨酸残基的方向，在活性和非活性构象之间切换，直接响应靶配体的结合来调节ATP酶活性。本文在由AAA+蛋白催化的生物学过程的背景下讨论了对ATP酶活性进行这种程度控制的原因。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/10fd/2806578/23344b16aac5/ukmss-2347-f0005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/10fd/2806578/1b3fece2951a/ukmss-2347-f0001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/10fd/2806578/27c9f08f3092/ukmss-2347-f0002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/10fd/2806578/3b66a9628289/ukmss-2347-f0003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/10fd/2806578/5c673541257c/ukmss-2347-f0004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/10fd/2806578/23344b16aac5/ukmss-2347-f0005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/10fd/2806578/1b3fece2951a/ukmss-2347-f0001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/10fd/2806578/27c9f08f3092/ukmss-2347-f0002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/10fd/2806578/3b66a9628289/ukmss-2347-f0003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/10fd/2806578/5c673541257c/ukmss-2347-f0004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/10fd/2806578/23344b16aac5/ukmss-2347-f0005.jpg

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