2lt4: Difference between revisions
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==CdnLNt from Myxoccoccus xanthus== | ==CdnLNt from Myxoccoccus xanthus== | ||
<StructureSection load='2lt4' size='340' side='right' caption='[[2lt4 | <StructureSection load='2lt4' size='340' side='right'caption='[[2lt4]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2lt4]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2lt4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Myxococcus_xanthus_DK_1622 Myxococcus xanthus DK 1622]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LT4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LT4 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">Solution NMR</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=2lt4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lt4 OCA], [https://pdbe.org/2lt4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lt4 RCSB], [https://www.ebi.ac.uk/pdbsum/2lt4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lt4 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q1D927_MYXXD Q1D927_MYXXD] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 2lt4" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Myxococcus xanthus DK 1622]] | ||
[[Category: | [[Category: Jimenez MA]] | ||
[[Category: | [[Category: Mirassou Y]] | ||
[[Category: | [[Category: Padmanabhan S]] | ||
Latest revision as of 08:51, 15 May 2024
CdnLNt from Myxoccoccus xanthusCdnLNt from Myxoccoccus xanthus
Structural highlights
FunctionPublication Abstract from PubMedCdnL and CarD are two functionally distinct members of the CarD_CdnL_TRCF family of bacterial RNA polymerase (RNAP)-interacting proteins, which co-exist in Myxococcus xanthus. While CarD, found exclusively in myxobacteria, has been implicated in the activity of various extracytoplasmic function (ECF) sigma-factors, the function and mode of action of the essential CdnL, whose homologs are widespread among bacteria, remain to be elucidated in M. xanthus. Here, we report the NMR solution structure of CdnL and present a structure-based mutational analysis of its function. An N-terminal five-stranded beta-sheet Tudor-like module in the two-domain CdnL mediates binding to RNAP-beta, and mutations that disrupt this interaction impair cell growth. The compact CdnL C-terminal domain consists of five alpha-helices folded as in some tetratricopeptide repeat-like protein-protein interaction domains, and contains a patch of solvent-exposed nonpolar and basic residues, among which a set of basic residues is shown to be crucial for CdnL function. We show that CdnL, but not its loss-of-function mutants, stabilizes formation of transcriptionally competent, open complexes by the primary sigmaA-RNAP holoenzyme at an rRNA promoter in vitro. Consistent with this, CdnL is present at rRNA promoters in vivo. Implication of CdnL in RNAP-sigmaA activity and of CarD in ECF-sigma function in M. xanthus exemplifies how two related members within a widespread bacterial protein family have evolved to enable distinct sigma-dependent promoter activity. Structural Insights into RNA Polymerase Recognition and Essential Function of Myxococcus xanthus CdnL.,Gallego-Garcia A, Mirassou Y, Garcia-Moreno D, Elias-Arnanz M, Jimenez MA, Padmanabhan S PLoS One. 2014 Oct 1;9(10):e108946. doi: 10.1371/journal.pone.0108946., eCollection 2014. PMID:25272012[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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