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| ==Structure of Mtb RNAP Beta subunit B1 and B2 domains== | | ==Structure of Mtb RNAP Beta subunit B1 and B2 domains== |
| <StructureSection load='4kbj' size='340' side='right' caption='[[4kbj]], [[Resolution|resolution]] 2.45Å' scene=''> | | <StructureSection load='4kbj' size='340' side='right'caption='[[4kbj]], [[Resolution|resolution]] 2.45Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[4kbj]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KBJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4KBJ FirstGlance]. <br> | | <table><tr><td colspan='2'>[[4kbj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KBJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KBJ FirstGlance]. <br> |
| </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MT0695, MTCI376.08c, rpoB, Rv0667 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 Mycobacterium tuberculosis])</td></tr> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4532Å</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=4kbj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kbj OCA], [https://pdbe.org/4kbj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kbj RCSB], [https://www.ebi.ac.uk/pdbsum/4kbj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kbj 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=4kbj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kbj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4kbj RCSB], [http://www.ebi.ac.uk/pdbsum/4kbj PDBsum]</span></td></tr> | |
| </table> | | </table> |
| == Function == | | == Function == |
| [[http://www.uniprot.org/uniprot/RPOB_MYCTU RPOB_MYCTU]] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.[HAMAP-Rule:MF_01321] | | [https://www.uniprot.org/uniprot/RPOB_MYCTU RPOB_MYCTU] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.[HAMAP-Rule:MF_01321] |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| CarD from Mycobacterium tuberculosis (Mtb) is an essential protein shown to be involved in stringent response through downregulation of rRNA and ribosomal protein genes. CarD interacts with the beta-subunit of RNAP and this interaction is vital for Mtb's survival during the persistent infection state. We have determined the crystal structure of CarD in complex with the RNAP beta-subunit beta1 and beta2 domains at 2.1 A resolution. The structure reveals the molecular basis of CarD/RNAP interaction, providing a basis to further our understanding of RNAP regulation by CarD. The structural fold of the CarD N-terminal domain is conserved in RNAP interacting proteins such as TRCF-RID and CdnL, and displays similar interactions to the predicted homology model based on the TRCF/RNAP beta1 structure. Interestingly, the structure of the C-terminal domain, which is required for complete CarD function in vivo, represents a distinct DNA-binding fold.
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| Structure of the Mtb CarD/RNAP beta-Lobes Complex Reveals the Molecular Basis of Interaction and Presents a Distinct DNA-Binding Domain for Mtb CarD.,Gulten G, Sacchettini JC Structure. 2013 Sep 17. pii: S0969-2126(13)00306-7. doi:, 10.1016/j.str.2013.08.014. PMID:24055315<ref>PMID:24055315</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| ==See Also== | | ==See Also== |
| *[[RNA polymerase|RNA polymerase]] | | *[[RNA polymerase 3D structures|RNA polymerase 3D structures]] |
| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: DNA-directed RNA polymerase]] | | [[Category: Large Structures]] |
| [[Category: Mycobacterium tuberculosis]] | | [[Category: Mycobacterium tuberculosis]] |
| [[Category: Gulten, G]] | | [[Category: Gulten G]] |
| [[Category: Sacchettini, J C]] | | [[Category: Sacchettini JC]] |
| [[Category: Structural genomic]]
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| [[Category: Card]]
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| [[Category: Dna]]
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| [[Category: Dna dependent rna polymerase]]
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| [[Category: Sigma factor]]
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| [[Category: Tbsgc]]
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| [[Category: Transferase]]
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| [[Category: Trcf]]
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