1t0x: Difference between revisions
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==MODEL OF THE BACTERIAL RNA POLYMERASE OPEN COMPLEX WITH THE SUBSTRATE AND PPGPP BOUND== | ==MODEL OF THE BACTERIAL RNA POLYMERASE OPEN COMPLEX WITH THE SUBSTRATE AND PPGPP BOUND== | ||
<StructureSection load='1t0x' size='340' side='right' caption='[[1t0x]]' scene=''> | <StructureSection load='1t0x' size='340' side='right'caption='[[1t0x]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1T0X FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1t0x FirstGlance], [https://www.ebi.ac.uk/pdbsum/1t0x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1t0x ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Theoretical Model]] | [[Category: Theoretical Model]] | ||
[[Category: Large Structures]] | |||
[[Category: Artsimovitch, I]] | [[Category: Artsimovitch, I]] | ||
[[Category: Hosaka, T]] | [[Category: Hosaka, T]] | ||
Latest revision as of 10:40, 22 September 2021
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MODEL OF THE BACTERIAL RNA POLYMERASE OPEN COMPLEX WITH THE SUBSTRATE AND PPGPP BOUNDMODEL OF THE BACTERIAL RNA POLYMERASE OPEN COMPLEX WITH THE SUBSTRATE AND PPGPP BOUND
Structural highlights
Publication Abstract from PubMedGuanosine-tetraphosphate (ppGpp) is a major regulator of stringent control, an adaptive response of bacteria to amino acid starvation. The 2.7 A resolution structure of the Thermus thermophilus RNA polymerase (RNAP) holoenzyme in complex with ppGpp reveals that ppGpp binds to the same site near the active center in both independent RNAP molecules in the crystal but in strikingly distinct orientations. Binding is symmetrical with respect to the two diphosphates of ppGpp and is relaxed with respect to the orientation of the nucleotide base. Different modes of ppGpp binding are coupled with asymmetry of the active site configurations. The results suggest that base pairing of ppGpp with cytosines in the nontemplate DNA strand might be an essential component of transcription control by ppGpp. We present experimental evidence highlighting the importance of base-specific contacts between ppGpp and specific cytosine residues during both transcription initiation and elongation. Structural basis for transcription regulation by alarmone ppGpp.,Artsimovitch I, Patlan V, Sekine S, Vassylyeva MN, Hosaka T, Ochi K, Yokoyama S, Vassylyev DG Cell. 2004 Apr 30;117(3):299-310. PMID:15109491[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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