Visualizing the ATPase cycle in a protein disaggregating machine: structural basis for substrate binding by ClpB.

Visualizing the ATPase cycle in a protein disaggregating machine: structural basis for substrate binding by ClpB. Research Abstract Details 

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Visualizing the ATPase cycle in a protein disaggregating machine: structural basis for substrate binding by ClpB. Abstract Text:

Sukyeong Lee,Jae-Mun Choi,Francis T F Tsai,

ClpB is a ring-shaped molecular chaperone that has the remarkable ability to disaggregate stress-damaged proteins. Here we present the electron cryomicroscopy reconstruction of an ATP-activated ClpB trap mutant, along with reconstructions of ClpB in the AMPPNP, ADP, and in the nucleotide-free state. We show that motif 2 of the ClpB M domain is positioned between the D1-large domains of neighboring subunits and could facilitate a concerted, ATP-driven conformational change in the AAA-1 ring. We further demonstrate biochemically that ATP is essential for high-affinity substrate binding to ClpB and cannot be substituted with AMPPNP. Our structures show that in the ATP-activated state, the D1 loops are stabilized at the central pore, providing the structural basis for high-affinity substrate binding. Taken together, our results support a mechanism by which ClpB captures substrates on the upper surface of the AAA-1 ring before threading them through the ClpB hexamer in an ATP hydrolysis-driven step.

Visualizing the ATPase cycle in a protein disaggregating machine: structural basis for substrate binding by ClpB. Publishing Authors By Initials

S Lee,JM Choi,FT Tsai,

For similar bacteria: gram-negative bacteria: gram-negative aerobic bacteria: gram-negative aerobic rods and cocci: thermus: thermus thermophilus research abstracts see: bacteria: gram-negative bacteria: gram-negative aerobic bacteria: gram-negative aerobic rods and cocci: thermus: thermus thermophilus research

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Visualizing the ATPase cycle in a protein disaggregating machine: structural basis for substrate binding by ClpB. Journal Published:

PUBLICATION TYPE: Research Support, U.S. Gov't,

Journal: Molecular cell

VOLUME: 25

Page Numbers: 261-71

Journal Abbreviation: Mol. Cell

ISSN: 1097-2765

DAY: 26

MONTH: Jan

YEAR: 2007

Visualizing the ATPase cycle in a protein disaggregating machine: structural basis for substrate binding by ClpB. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 9802571

Visualizing the ATPase cycle in a protein disaggregating machine: structural basis for substrate binding by ClpB. Keywords Mesh Terms:

KEYWORDS: Thermus thermophilus

MESH TERMS: metabolism

Chemical & Substance for Abstract: Visualizing the ATPase cycle in a protein disaggregating machine: structural basis for substrate binding by ClpB. Information

Substance Name: Adenosine Triphosphatases

Registry Number: EC 3.6.1.-

Grant and Affiliation Information for Visualizing the ATPase cycle in a protein disaggregating machine: structural basis for substrate binding by ClpB.

AFFILIATION: Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, USA.

Country: United States

AGENCY: United States NIGMS

GRANT: R01 GM067672-04

ACRONYM: GM

MEDLINETA: Mol Cell

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