4mq9: Difference between revisions
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<StructureSection load='4mq9' size='340' side='right'caption='[[4mq9]], [[Resolution|resolution]] 3.35Å' scene=''> | <StructureSection load='4mq9' size='340' side='right'caption='[[4mq9]], [[Resolution|resolution]] 3.35Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4mq9]] is a 7 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4mq9]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Actinomadura_sp. Actinomadura sp.] and [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MQ9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MQ9 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.35Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0QZ:D-ISOSERINE'>0QZ</scene>, <scene name='pdbligand=2RA:3-AMINO-D-ALANINE'>2RA</scene>, <scene name='pdbligand=2TL:D-ALLOTHREONINE'>2TL</scene>, <scene name='pdbligand=DSN:D-SERINE'>DSN</scene>, <scene name='pdbligand=DVA:D-VALINE'>DVA</scene>, <scene name='pdbligand=FGL:2-AMINOPROPANEDIOIC+ACID'>FGL</scene>, <scene name='pdbligand=MB8:(2Z)-2-METHYLBUT-2-ENOIC+ACID'>MB8</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=R2T:BETA,GAMMA-DIHYDROXYGLUTAMINE'>R2T</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=4mq9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mq9 OCA], [https://pdbe.org/4mq9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mq9 RCSB], [https://www.ebi.ac.uk/pdbsum/4mq9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mq9 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/RPOA_THET8 RPOA_THET8] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 23: | Line 21: | ||
==See Also== | ==See Also== | ||
*[[RNA polymerase|RNA polymerase]] | *[[RNA polymerase 3D structures|RNA polymerase 3D structures]] | ||
*[[Sigma factor|Sigma factor]] | *[[Sigma factor 3D structures|Sigma factor 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 30: | Line 28: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Actinomadura sp]] | [[Category: Actinomadura sp]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Thermus thermophilus | [[Category: Thermus thermophilus HB8]] | ||
[[Category: Arnold E]] | |||
[[Category: Arnold | [[Category: Ebright RH]] | ||
[[Category: Ebright | [[Category: Ho MX]] | ||
[[Category: Ho | [[Category: Tuske S]] | ||
[[Category: Tuske | [[Category: Zhang Y]] | ||
[[Category: Zhang | |||
Latest revision as of 19:40, 20 September 2023
Crystal structure of Thermus thermophilus RNA polymerase holoenzyme in complex with GE23077Crystal structure of Thermus thermophilus RNA polymerase holoenzyme in complex with GE23077
Structural highlights
FunctionRPOA_THET8 DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Publication Abstract from PubMedUsing a combination of genetic, biochemical, and structural approaches, we show that the cyclic-peptide antibiotic GE23077 (GE) binds directly to the bacterial RNA polymerase (RNAP) active-center 'i' and 'i+1' nucleotide binding sites, preventing the binding of initiating nucleotides, and thereby preventing transcription initiation. The target-based resistance spectrum for GE is unusually small, reflecting the fact that the GE binding site on RNAP includes residues of the RNAP active center that cannot be substituted without loss of RNAP activity. The GE binding site on RNAP is different from the rifamycin binding site. Accordingly, GE and rifamycins do not exhibit cross-resistance, and GE and a rifamycin can bind simultaneously to RNAP. The GE binding site on RNAP is immediately adjacent to the rifamycin binding site. Accordingly, covalent linkage of GE to a rifamycin provides a bipartite inhibitor having very high potency and very low susceptibility to target-based resistance. DOI: http://dx.doi.org/10.7554/eLife.02450.001. GE23077 binds to the RNA polymerase 'i' and 'i+1' sites and prevents the binding of initiating nucleotides.,Zhang Y, Degen D, Ho MX, Sineva E, Ebright KY, Ebright YW, Mekler V, Vahedian-Movahed H, Feng Y, Yin R, Tuske S, Irschik H, Jansen R, Maffioli S, Donadio S, Arnold E, Ebright RH Elife. 2014 Jan 1;3:e02450. doi: 10.7554/eLife.02450. PMID:24755292[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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