2vii

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Revision as of 08:57, 23 January 2008

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spinqualitylabelsall models 2vii, resolution 2.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

PSPF1-275-MG-AMP

Overview

Mechanochemical proteins rely on ATP hydrolysis to establish the different, functional states required for their biological output. Studying the, transient functional intermediate states these proteins adopt as they, progress through the ATP hydrolysis cycle is key to understanding the, molecular basis of their mechanism. Many of these intermediates have been, successfully 'trapped' and functionally characterised using ATP analogues., Here, we present a new nucleotide analogue, AMP-AlF(x), which traps PspF, a bacterial enhancer binding protein, in a stable complex with the, sigma(54)-RNA polymerase holoenzyme. The crystal structure of, AMP-AlF(x)*PspF(1-275) provides new information on protein-nucleotide, interactions and suggests that the beta and gamma phosphates are more, important than the alpha phosphate in terms of sensing nucleotide bound, states. In addition, functional data obtained with AMP-AlF(x) establish, distinct roles for the conserved catalytic AAA(+) (ATPases associated with, various cellular activities) residues, suggesting that AMP-AlF(x) is a, powerful new tool to study AAA(+) protein family members and, more, generally, Walker motif ATPases.

About this Structure

2VII is a Single protein structure of sequence from Escherichia coli with and as ligands. Known structural/functional Sites: and . Full crystallographic information is available from OCA.

Reference

Trapping of a transcription complex using a new nucleotide analogue: AMP aluminium fluoride., Joly N, Rappas M, Buck M, Zhang X, J Mol Biol. 2008 Feb 1;375(5):1206-11. Epub 2007 Nov 22. PMID:18082766

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