pubmed-article:16122422 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:16122422 | lifeskim:mentions | umls-concept:C0035681 | lld:lifeskim |
pubmed-article:16122422 | lifeskim:mentions | umls-concept:C0035692 | lld:lifeskim |
pubmed-article:16122422 | lifeskim:mentions | umls-concept:C0021467 | lld:lifeskim |
pubmed-article:16122422 | lifeskim:mentions | umls-concept:C0026377 | lld:lifeskim |
pubmed-article:16122422 | lifeskim:mentions | umls-concept:C0021469 | lld:lifeskim |
pubmed-article:16122422 | lifeskim:mentions | umls-concept:C0075300 | lld:lifeskim |
pubmed-article:16122422 | pubmed:issue | 4 | lld:pubmed |
pubmed-article:16122422 | pubmed:dateCreated | 2005-8-26 | lld:pubmed |
pubmed-article:16122422 | pubmed:abstractText | 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. | lld:pubmed |
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pubmed-article:16122422 | pubmed:language | eng | lld:pubmed |
pubmed-article:16122422 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16122422 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:16122422 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:16122422 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:16122422 | pubmed:month | Aug | lld:pubmed |
pubmed-article:16122422 | pubmed:issn | 0092-8674 | lld:pubmed |
pubmed-article:16122422 | pubmed:author | pubmed-author:EbrightRichar... | lld:pubmed |
pubmed-article:16122422 | pubmed:author | pubmed-author:DhariaChhayaC | lld:pubmed |
pubmed-article:16122422 | pubmed:author | pubmed-author:ArnoldEddyE | lld:pubmed |
pubmed-article:16122422 | pubmed:author | pubmed-author:SarafianosSte... | lld:pubmed |
pubmed-article:16122422 | pubmed:author | pubmed-author:MukhopadhyayJ... | lld:pubmed |
pubmed-article:16122422 | pubmed:author | pubmed-author:LaptenkoOlegO | lld:pubmed |
pubmed-article:16122422 | pubmed:author | pubmed-author:LeeJookyungJ | lld:pubmed |
pubmed-article:16122422 | pubmed:author | pubmed-author:BorukhovSerge... | lld:pubmed |
pubmed-article:16122422 | pubmed:author | pubmed-author:ClarkArthur... | lld:pubmed |
pubmed-article:16122422 | pubmed:author | pubmed-author:BirktoftJens... | lld:pubmed |
pubmed-article:16122422 | pubmed:author | pubmed-author:HudsonBrianB | lld:pubmed |
pubmed-article:16122422 | pubmed:author | pubmed-author:LeroyOlivierO | lld:pubmed |
pubmed-article:16122422 | pubmed:author | pubmed-author:SinevaElenaE | lld:pubmed |