4kmc
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4kmc]] is a 1 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=4KMC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KMC FirstGlance]. <br> | <table><tr><td colspan='2'>[[4kmc]] is a 1 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=4KMC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KMC 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=4kmc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kmc OCA], [https://pdbe.org/4kmc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kmc RCSB], [https://www.ebi.ac.uk/pdbsum/4kmc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kmc 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]] 2.15Å</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=4kmc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kmc OCA], [https://pdbe.org/4kmc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kmc RCSB], [https://www.ebi.ac.uk/pdbsum/4kmc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kmc ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/CARD_MYCTU CARD_MYCTU] Controls rRNA transcription by binding to the RNA polymerase (RNAP). Required for replication and persistence during infection of mice.<ref>PMID:19596241</ref> <ref>PMID:22904282</ref> | [https://www.uniprot.org/uniprot/CARD_MYCTU CARD_MYCTU] Controls rRNA transcription by binding to the RNA polymerase (RNAP). Required for replication and persistence during infection of mice.<ref>PMID:19596241</ref> <ref>PMID:22904282</ref> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The CarD protein is highly expressed in mycobacterial strains under basal conditions and is transcriptionally induced during multiple types of genotoxic stress and starvation. The CarD protein binds the beta subunit of RNA polymerase and influences gene expression. The disruption of interactions between CarD and the beta subunit of RNA polymerase has a significant effect on mycobacterial survival, resistance to stress and pathogenesis. To understand the structure of CarD and its interaction with the beta subunit of RNA polymerase, Mycobacterium tuberculosis CarD (MtbCarD) and the Thermus aquaticus RNA polymerase beta subunit were recombinantly expressed and purified. Secondary-structure analysis using circular-dichroism spectroscopy indicated that MtbCarD contains approximately 60% alpha-helix, approximately 7% beta-sheet and approximately 33% random-coil structure. The C-terminal domain of MtbCarD (CarD(83-161)) was crystallized and its X-ray structure was determined at 2.1 A resolution. CarD(83-161) forms a distorted Y-shaped structure containing bundles of three helices connected by a loop. The residues forming the distorted Y-shaped structure are highly conserved in CarD sequences from other mycobacterial species. Comparison of the CarD(83-161) structure with the recently determined full-length M. tuberculosis and T. thermophilus CarD crystal structures revealed structural differences in residues 141-161 of the C-terminal domain of the CarD(83-161) structure. The structural changes in the CarD(83-161) structure occurred owing to proteolysis and crystallization artifacts. | ||
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| - | Structure of the carboxy-terminal domain of Mycobacterium tuberculosis CarD protein: an essential rRNA transcriptional regulator.,Gangwar SP, Meena SR, Saxena AK Acta Crystallogr F Struct Biol Commun. 2014 Feb;70(Pt 2):160-5. doi:, 10.1107/S2053230X13034407. Epub 2014 Jan 21. PMID:24637748<ref>PMID:24637748</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4kmc" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
Structure analysis of M. Tuberculosis rRNA transcriptional regulator CarD and its interaction with T. Aquaticus RNA polymerase-BETA1 domain
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