4kbj: Difference between revisions

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 == Structural highlights ==
 <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='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>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4532&#8491;</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>
 </table>
 == Function ==
 [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;">
-== Publication Abstract from PubMed ==
-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.
-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>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 4kbj" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[RNA polymerase 3D structures|RNA polymerase 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>