Making the Right Moves

Mario A. Bianchet; L. Mario Amzel

doi:10.1016/j.str.2007.07.004

Making the Right Moves

Mario A. Bianchet, L. Mario Amzel

School of Medicine

Research output: Contribution to journal › Short survey › peer-review

1 Scopus citations

Abstract

The structure of the nucleotide-free F₁-ATPase from a thermoalkaliphilic bacterium presented in this issue of Structure (Stocker et al., 2007) reveals the structural interactions that prevent the enzyme from operating naturally in the hydrolytic direction. The data provide new insights into the mechanism of the F_oF₁-ATP synthase.

Original language	English (US)
Pages (from-to)	885-886
Number of pages	2
Journal	Structure
Volume	15
Issue number	8
DOIs	https://doi.org/10.1016/j.str.2007.07.004
State	Published - Aug 14 2007

ASJC Scopus subject areas

Structural Biology
Molecular Biology

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10.1016/j.str.2007.07.004

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title = "Making the Right Moves",

abstract = "The structure of the nucleotide-free F1-ATPase from a thermoalkaliphilic bacterium presented in this issue of Structure (Stocker et al., 2007) reveals the structural interactions that prevent the enzyme from operating naturally in the hydrolytic direction. The data provide new insights into the mechanism of the FoF1-ATP synthase.",

author = "Bianchet, {Mario A.} and Amzel, {L. Mario}",

year = "2007",

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doi = "10.1016/j.str.2007.07.004",

language = "English (US)",

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journal = "Structure",

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AU - Bianchet, Mario A.

AU - Amzel, L. Mario

PY - 2007/8/14

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N2 - The structure of the nucleotide-free F1-ATPase from a thermoalkaliphilic bacterium presented in this issue of Structure (Stocker et al., 2007) reveals the structural interactions that prevent the enzyme from operating naturally in the hydrolytic direction. The data provide new insights into the mechanism of the FoF1-ATP synthase.

AB - The structure of the nucleotide-free F1-ATPase from a thermoalkaliphilic bacterium presented in this issue of Structure (Stocker et al., 2007) reveals the structural interactions that prevent the enzyme from operating naturally in the hydrolytic direction. The data provide new insights into the mechanism of the FoF1-ATP synthase.

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DO - 10.1016/j.str.2007.07.004

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C2 - 17697991

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SN - 0969-2126

VL - 15

SP - 885

EP - 886

JO - Structure

JF - Structure

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ER -

Making the Right Moves

Abstract

ASJC Scopus subject areas

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