Crystal structures of the pilus retraction motor PilT suggest large domain movements and subunit cooperation drive motility.

Crystal structures of the pilus retraction motor PilT suggest large domain movements and subunit cooperation drive motility. Research Abstract Details 

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Crystal structures of the pilus retraction motor PilT suggest large domain movements and subunit cooperation drive motility. Abstract Text:

PilT is a hexameric ATPase required for bacterial type IV pilus retraction and surface motility. Crystal structures of ADP- and ATP-bound Aquifex aeolicus PilT at 2.8 and 3.2 A resolution show N-terminal PAS-like and C-terminal RecA-like ATPase domains followed by a set of short C-terminal helices. The hexamer is formed by extensive polar subunit interactions between the ATPase core of one monomer and the N-terminal domain of the next. An additional structure captures a nonsymmetric PilT hexamer in which approach of invariant arginines from two subunits to the bound nucleotide forms an enzymatically competent active site. A panel of pilT mutations highlights the importance of the arginines, the PAS-like domain, the polar subunit interface, and the C-terminal helices for retraction. We present a model for ATP binding leading to dramatic PilT domain motions, engagement of the arginine wire, and subunit communication in this hexameric motor. Our conclusions apply to the entire type II/IV secretion ATPase family.

Crystal structures of the pilus retraction motor PilT suggest large domain movements and subunit cooperation drive motility. Publishing Authors By Initials

For similar proteins: protein subunits research abstracts see: proteins: protein subunits research

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Crystal structures of the pilus retraction motor PilT suggest large domain movements and subunit cooperation drive motility. Journal Published:

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

Journal: Structure (London, England : 1993)

VOLUME: 15

Page Numbers: 363-76

Journal Abbreviation: Structure

ISSN: 0969-2126

DAY: 3

MONTH: Mar

YEAR: 2007

Crystal structures of the pilus retraction motor PilT suggest large domain movements and subunit cooperation drive motility. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 101087697

Crystal structures of the pilus retraction motor PilT suggest large domain movements and subunit cooperation drive motility. Keywords Mesh Terms:

KEYWORDS: Protein Subunits

MESH TERMS: physiology

Chemical & Substance for Abstract: Crystal structures of the pilus retraction motor PilT suggest large domain movements and subunit cooperation drive motility. Information

Substance Name: pilT protein, bacteria

Registry Number: EC 3.6.1.-

Grant and Affiliation Information for Crystal structures of the pilus retraction motor PilT suggest large domain movements and subunit cooperation drive motility.

AFFILIATION: Department of Bacteriology, University of Wisconsin-Madison, Madison, WI 53706, USA.

Country: United States

AGENCY: United States NIGMS

GRANT: R01 GM059721-05

ACRONYM: GM

MEDLINETA: Structure

REFSOURCE: Structure. 2007 Mar;15(3):255-7

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