A Proposed Common Allosteric Mechanism for Active Transport, Muscle Contraction, and Ribosomal Translocation

Overview

Journal Proc Natl Acad Sci U S A

Specialty Science

Date 1969 Sep 1

PMID 5263010

Citations 10

Authors

T L Hill

Affiliations

Soon will be listed here.

Abstract

It is suggested that active transport, muscle contraction, and ribosomal translocation may all make use of a common allosteric mechanism in which ATP or GTP serves as both the effector and substrate and in which a conformational change in a protein (enzyme) moves or exerts a force on a second ligand. The enzymatic splitting of ATP or GTP provides the driving force for the process and allows repetition of the steady-state cycle.

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DNA-strand exchange promoted by RecA protein in the absence of ATP: implications for the mechanism of energy transduction in protein-promoted nucleic acid transactions.

Kowalczykowski S, Krupp R Proc Natl Acad Sci U S A. 1995; 92(8):3478-82.

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Phosphate exchange in the pit transport system in Escherichia coli.

Rosenberg H, Russell L, Jacomb P, Chegwidden K J Bacteriol. 1982; 149(1):123-30.

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The relation between calcium and contraction kinetics in skinned muscle fibres.

PODOLSKY R, Teichholz L J Physiol. 1970; 211(1):19-35.

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Analysis of a model for active transport.

Hill T Proc Natl Acad Sci U S A. 1970; 65(2):409-16.

PMID: 5263773 PMC: 282918. DOI: 10.1073/pnas.65.2.409.

References

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