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Cation-π interactions induce kinking of a molecular hinge in the RNA polymerase bridge-helix domain

Heindl, Hans and Greenwell, Pamela and Weingarten, Noam and Kiss, Tamas and Terstyanszky, Gabor and Weinzierl, Robert O.J. (2011) Cation-π interactions induce kinking of a molecular hinge in the RNA polymerase bridge-helix domain. Biochemical Society Transactions, 39 (1). pp. 31-35. ISSN 0300-5127

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Official URL: http://dx.doi.org/10.1042/BST0390031

Abstract

RNAPs (RNA polymerases) are complex molecular machines that contain a highly conserved catalytic site surrounded by conformationally flexible domains. High-throughput mutagenesis in the archaeal model system Methanocaldococcus jannaschii has demonstrated that the nanomechanical properties of one of these domains, the bridge-helix, exert a key regulatory role on the rate of the NAC (nucleotide-addition cycle). Mutations that increase the probability and/or half-life of kink formation in the BH-HC (bridge-helix C-terminal hinge) cause a substantial increase in specific activity ('superactivity'). Fully atomistic molecular dynamics simulations show that kinking of the BH-HC appears to be driven by cation-π interactions and involve amino acid side chains that are exceptionally highly conserved in all prokaryotic and eukaryotic species.

Item Type:Article
Research Community:University of Westminster > Life Sciences, School of
University of Westminster > Electronics and Computer Science, School of
ID Code:9101
Deposited On:28 Jan 2011 09:44
Last Modified:28 Jan 2011 09:44

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