|
|
| (One intermediate revision by the same user not shown) |
| Line 3: |
Line 3: |
| <SX load='6j9e' size='340' side='right' viewer='molstar' caption='[[6j9e]], [[Resolution|resolution]] 3.41Å' scene=''> | | <SX load='6j9e' size='340' side='right' viewer='molstar' caption='[[6j9e]], [[Resolution|resolution]] 3.41Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[6j9e]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Xanoo Xanoo], [http://en.wikipedia.org/wiki/Xanop Xanop] and [http://en.wikipedia.org/wiki/Xanthomonas_campestris_phage_xp10 Xanthomonas campestris phage xp10]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6J9E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6J9E FirstGlance]. <br> | | <table><tr><td colspan='2'>[[6j9e]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Xanthomonas_oryzae_pv._oryzae Xanthomonas oryzae pv. oryzae], [https://en.wikipedia.org/wiki/Xanthomonas_oryzae_pv._oryzae_PXO99A Xanthomonas oryzae pv. oryzae PXO99A], [https://en.wikipedia.org/wiki/Xanthomonas_virus_Xp10 Xanthomonas virus Xp10] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6J9E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6J9E FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.41Å</td></tr> |
| <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rpoA, PXO_04496 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=360094 XANOP]), rpoB, PXO_04530 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=360094 XANOP]), rpoC, PXO_04529 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=360094 XANOP]), rpoZ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=64187 XANOO]), nusA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=360094 XANOP])</td></tr> | | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA-directed_RNA_polymerase DNA-directed RNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.6 2.7.7.6] </span></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=6j9e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6j9e OCA], [https://pdbe.org/6j9e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6j9e RCSB], [https://www.ebi.ac.uk/pdbsum/6j9e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6j9e ProSAT]</span></td></tr> |
| <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6j9e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6j9e OCA], [http://pdbe.org/6j9e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6j9e RCSB], [http://www.ebi.ac.uk/pdbsum/6j9e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6j9e ProSAT]</span></td></tr> | |
| </table> | | </table> |
| == Function == | | == Function == |
| [[http://www.uniprot.org/uniprot/RPOC_XANOP RPOC_XANOP]] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. [[http://www.uniprot.org/uniprot/RPOB_XANOP RPOB_XANOP]] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. [[http://www.uniprot.org/uniprot/RPOA_XANOP RPOA_XANOP]] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. [[http://www.uniprot.org/uniprot/A0A0U4VN94_XANOO A0A0U4VN94_XANOO]] Promotes RNA polymerase assembly. Latches the N- and C-terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits.[HAMAP-Rule:MF_00366][SAAS:SAAS00387808] | | [https://www.uniprot.org/uniprot/RPOA_XANOP RPOA_XANOP] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. |
| <div style="background-color:#fffaf0;">
| |
| == Publication Abstract from PubMed ==
| |
| Bacteriophages typically hijack the host bacterial transcriptional machinery to regulate their own gene expression and that of the host bacteria. The structural basis for bacteriophage protein-mediated transcription regulation-in particular transcription antitermination-is largely unknown. Here we report the 3.4 A and 4.0 A cryo-EM structures of two bacterial transcription elongation complexes (P7-NusA-TEC and P7-TEC) comprising the bacteriophage protein P7, a master host-transcription regulator encoded by bacteriophage Xp10 of the rice pathogen Xanthomonas oryzae pv. Oryzae (Xoo) and discuss the mechanisms by which P7 modulates the host bacterial RNAP. The structures together with biochemical evidence demonstrate that P7 prevents transcription termination by plugging up the RNAP RNA-exit channel and impeding RNA-hairpin formation at the intrinsic terminator. Moreover, P7 inhibits transcription initiation by restraining RNAP-clamp motions. Our study reveals the structural basis for transcription antitermination by phage proteins and provides insights into bacterial transcription regulation.
| |
| | |
| Structural basis for transcription antitermination at bacterial intrinsic terminator.,You L, Shi J, Shen L, Li L, Fang C, Yu C, Cheng W, Feng Y, Zhang Y Nat Commun. 2019 Jul 11;10(1):3048. doi: 10.1038/s41467-019-10955-x. PMID:31296855<ref>PMID:31296855</ref>
| |
| | |
| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| |
| </div>
| |
| <div class="pdbe-citations 6j9e" style="background-color:#fffaf0;"></div>
| |
|
| |
|
| ==See Also== | | ==See Also== |
| *[[RNA polymerase 3D structures|RNA polymerase 3D structures]] | | *[[RNA polymerase 3D structures|RNA polymerase 3D structures]] |
| == References ==
| |
| <references/>
| |
| __TOC__ | | __TOC__ |
| </SX> | | </SX> |
| [[Category: DNA-directed RNA polymerase]]
| |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Xanoo]] | | [[Category: Synthetic construct]] |
| [[Category: Xanop]] | | [[Category: Xanthomonas oryzae pv. oryzae]] |
| [[Category: Xanthomonas campestris phage xp10]] | | [[Category: Xanthomonas oryzae pv. oryzae PXO99A]] |
| [[Category: You, L L]] | | [[Category: Xanthomonas virus Xp10]] |
| [[Category: Zhang, Y]] | | [[Category: You LL]] |
| [[Category: Anti-termination]] | | [[Category: Zhang Y]] |
| [[Category: Nusa]]
| |
| [[Category: P7]]
| |
| [[Category: Phage]]
| |
| [[Category: Rna polymerase]]
| |
| [[Category: Rnap clamp]]
| |
| [[Category: Transcription]]
| |
| [[Category: Transcription initiation]]
| |
| [[Category: Transcription termination]]
| |
| [[Category: Xanthomonos oryzae]]
| |
| [[Category: Xp10]]
| |