1t0x

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{{Theoretical_model}}
{{Theoretical_model}}
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{{Seed}}
 
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[[Image:1t0x.png|left|200px]]
 
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==MODEL OF THE BACTERIAL RNA POLYMERASE OPEN COMPLEX WITH THE SUBSTRATE AND PPGPP BOUND==
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The line below this paragraph, containing "STRUCTURE_1t0x", creates the "Structure Box" on the page.
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<StructureSection load='1t0x' size='340' side='right'caption='[[1t0x]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<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>
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or leave the SCENE parameter empty for the default display.
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</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>
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</table>
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{{STRUCTURE_1t0x| PDB=1t0x | SCENE= }}
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Guanosine-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.
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===MODEL OF THE BACTERIAL RNA POLYMERASE OPEN COMPLEX WITH THE SUBSTRATE AND PPGPP BOUND===
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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<ref>PMID:15109491</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_15109491}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1t0x" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 15109491 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_15109491}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Theoretical Model]]
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Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T0X OCA].
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[[Category: Large Structures]]
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==Reference==
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<ref group="xtra">PMID:15109491</ref><references group="xtra"/>
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[[Category: Artsimovitch, I]]
[[Category: Artsimovitch, I]]
[[Category: Hosaka, T]]
[[Category: Hosaka, T]]
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[[Category: Vassylyeva, M N]]
[[Category: Vassylyeva, M N]]
[[Category: Yokoyama, S]]
[[Category: Yokoyama, S]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr 8 09:07:29 2010''
 

Current revision

Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.

MODEL OF THE BACTERIAL RNA POLYMERASE OPEN COMPLEX WITH THE SUBSTRATE AND PPGPP BOUND

PDB ID 1t0x

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