2mc5
From Proteopedia
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<StructureSection load='2mc5' size='340' side='right' caption='[[2mc5]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''> | <StructureSection load='2mc5' size='340' side='right' caption='[[2mc5]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | [[2mc5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Xanthomonas_campestris_phage_xp10 Xanthomonas campestris phage xp10]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MC5 OCA]. <br> | + | <table><tr><td colspan='2'>[[2mc5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Xanthomonas_campestris_phage_xp10 Xanthomonas campestris phage xp10]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MC5 OCA]. <br> |
| - | <b>[[Related_structure|Related:]]</b> [[2mc6|2mc6]]< | + | </td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2mc6|2mc6]]</td></tr> |
| - | <b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span>< | + | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr> |
| - | <b>Resources:</b> <span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2mc5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mc5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2mc5 RCSB], [http://www.ebi.ac.uk/pdbsum/2mc5 PDBsum]</span>< | + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2mc5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mc5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2mc5 RCSB], [http://www.ebi.ac.uk/pdbsum/2mc5 PDBsum]</span></td></tr> |
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Bacteriophages (phages) appropriate essential processes of bacterial hosts to benefit their own development. The multisubunit bacterial RNA polymerase (RNAp) enzyme, which catalyses DNA transcription, is targeted by phage-encoded transcription regulators that selectively modulate its activity. Here, we describe the structural and mechanistic basis for the inhibition of bacterial RNAp by the transcription regulator P7 encoded by Xanthomonas oryzae phage Xp10. We reveal that P7 uses a two-step mechanism to simultaneously interact with the catalytic beta and beta' subunits of the bacterial RNAp and inhibits transcription initiation by inducing the displacement of the sigma70-factor on initial engagement of RNAp with promoter DNA. The new mode of interaction with and inhibition mechanism of bacterial RNAp by P7 underscore the remarkable variety of mechanisms evolved by phages to interfere with host transcription. | Bacteriophages (phages) appropriate essential processes of bacterial hosts to benefit their own development. The multisubunit bacterial RNA polymerase (RNAp) enzyme, which catalyses DNA transcription, is targeted by phage-encoded transcription regulators that selectively modulate its activity. Here, we describe the structural and mechanistic basis for the inhibition of bacterial RNAp by the transcription regulator P7 encoded by Xanthomonas oryzae phage Xp10. We reveal that P7 uses a two-step mechanism to simultaneously interact with the catalytic beta and beta' subunits of the bacterial RNAp and inhibits transcription initiation by inducing the displacement of the sigma70-factor on initial engagement of RNAp with promoter DNA. The new mode of interaction with and inhibition mechanism of bacterial RNAp by P7 underscore the remarkable variety of mechanisms evolved by phages to interfere with host transcription. | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 09:33, 1 May 2014
A bacteriophage transcription regulator inhibits bacterial transcription initiation by -factor displacement
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