1xpr
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(New page: 200px<br /><applet load="1xpr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xpr, resolution 3.15Å" /> '''Structural mechanism...)
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Revision as of 04:07, 21 November 2007
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Structural mechanism of inhibition of the Rho transcription termination factor by the antibiotic 5a-formylbicyclomycin (FB)
Overview
Rho is a hexameric RNA/DNA helicase/translocase that terminates, transcription of select genes in bacteria. The naturally occurring, antibiotic, bicyclomycin (BCM), acts as a noncompetitive inhibitor of ATP, turnover to disrupt this process. We have determined three independent, X-ray crystal structures of Rho complexed with BCM and two semisynthetic, derivatives, 5a-(3-formylphenylsulfanyl)-dihydrobicyclomycin (FPDB) and, 5a-formylbicyclomycin (FB) to 3.15, 3.05, and 3.15 A resolution, respectively. The structures show that BCM and its derivatives are, nonnucleotide inhibitors that interact with Rho at a pocket adjacent to, the ATP and RNA binding sites in the C-terminal half of the protein. BCM, association prevents ATP turnover by an unexpected mechanism, occluding, the binding of the nucleophilic water molecule required for ATP, hydrolysis. Our data explain why only certain elements of BCM have been, amenable to modification and serve as a template for the design of new, inhibitors.
About this Structure
1XPR is a Single protein structure of sequence from Escherichia coli with MG, AGS and FB as ligands. Full crystallographic information is available from OCA.
Reference
Structural mechanism of inhibition of the Rho transcription termination factor by the antibiotic bicyclomycin., Skordalakes E, Brogan AP, Park BS, Kohn H, Berger JM, Structure. 2005 Jan;13(1):99-109. PMID:15642265
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