1zyr: Difference between revisions

Revision as of 16:33, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1zyr.png

Template:STRUCTURE 1zyr

Structure of Thermus thermophilus RNA polymerase holoenzyme in complex with the antibiotic streptolydiginStructure of Thermus thermophilus RNA polymerase holoenzyme in complex with the antibiotic streptolydigin

Template:ABSTRACT PUBMED 16122422

About this StructureAbout this Structure

1ZYR is a Protein complex structure of sequences from Thermus thermophilus. Full crystallographic information is available from OCA.

ReferenceReference

Inhibition of bacterial RNA polymerase by streptolydigin: stabilization of a straight-bridge-helix active-center conformation., Tuske S, Sarafianos SG, Wang X, Hudson B, Sineva E, Mukhopadhyay J, Birktoft JJ, Leroy O, Ismail S, Clark AD Jr, Dharia C, Napoli A, Laptenko O, Lee J, Borukhov S, Ebright RH, Arnold E, Cell. 2005 Aug 26;122(4):541-52. PMID:16122422

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Structure of Thermus thermophilus RNA polymerase holoenzyme in complex with the antibiotic streptolydigin'''
+===Structure of Thermus thermophilus RNA polymerase holoenzyme in complex with the antibiotic streptolydigin===
-==Overview==
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-We define the target, mechanism, and structural basis of inhibition of bacterial RNA polymerase (RNAP) by the tetramic acid antibiotic streptolydigin (Stl). Stl binds to a site adjacent to but not overlapping the RNAP active center and stabilizes an RNAP-active-center conformational state with a straight-bridge helix. The results provide direct support for the proposals that alternative straight-bridge-helix and bent-bridge-helix RNAP-active-center conformations exist and that cycling between straight-bridge-helix and bent-bridge-helix RNAP-active-center conformations is required for RNAP function. The results set bounds on models for RNAP function and suggest strategies for design of novel antibacterial agents.
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+{{ABSTRACT_PUBMED_16122422}}
 ==About this Structure==
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 [[Category: Streptolydigin]]
 [[Category: Transcription]]
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