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2lt1

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Revision as of 17:22, 18 January 2017

Solution NMR structure of the 72-residue N-terminal domain of Myxococcus xanthus CarD

Structural highlights

2lt1 is a 1 chain structure with sequence from Atcc 25232. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	carD (ATCC 25232)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

Two prototypes of the large CarD_CdnL_TRCF family of bacterial RNA polymerase (RNAP)-binding proteins, Myxococcus xanthus CarD and CdnL, have distinct functions whose molecular basis remain elusive. CarD, a global regulator linked to the action of several extracytoplasmic function (ECF) sigma-factors, binds to the RNAP beta subunit (RNAP-beta) and to protein CarG via an N-terminal domain, CarDNt, and to DNA via an intrinsically unfolded C-terminal domain resembling eukaryotic high-mobility-group A (HMGA) proteins. CdnL, a CarDNt-like protein that is essential for cell viability, is implicated in sigmaA-dependent rRNA promoter activation and interacts with RNAP-beta but not with CarG. While the HMGA-like domain of CarD by itself is inactive, we find that CarDNt has low but observable ability to activate ECF sigma-dependent promoters in vivo, indicating that the C-terminal DNA-binding domain is required to maximize activity. Our structure-function dissection of CarDNt reveals an N-terminal, five-stranded beta -sheet Tudor-like domain, CarD1-72, whose structure and contacts with RNAP-beta mimic those of CdnL. Intriguingly, and in marked contrast to CdnL, CarD mutations that disrupt its interaction with RNAP-beta did not annul activity. Our data suggest that the CarDNt C-terminal segment, CarD61-179, may be structurally distinct from its CdnL counterpart, and that it houses at least two distinct and crucial function determinants: (a) CarG-binding, which is specific to CarD; and (b) a basic residue stretch, which is also conserved and functionally required in CdnL. This study highlights the evolution of shared and divergent interactions in similar protein modules that enable the distinct activities of two related members of a functionally important and widespread bacterial protein family.

Structure-Function Dissection of Myxococcus xanthus CarD N-Terminal Domain, a Defining Member of the CarD_CdnL_TRCF Family of RNA Polymerase Interacting Proteins.,Bernal-Bernal D, Gallego-Garcia A, Garcia-Martinez G, Garcia-Heras F, Jimenez MA, Padmanabhan S, Elias-Arnanz M PLoS One. 2015 Mar 26;10(3):e0121322. doi: 10.1371/journal.pone.0121322., eCollection 2015. PMID:25811865^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Bernal-Bernal D, Gallego-Garcia A, Garcia-Martinez G, Garcia-Heras F, Jimenez MA, Padmanabhan S, Elias-Arnanz M. Structure-Function Dissection of Myxococcus xanthus CarD N-Terminal Domain, a Defining Member of the CarD_CdnL_TRCF Family of RNA Polymerase Interacting Proteins. PLoS One. 2015 Mar 26;10(3):e0121322. doi: 10.1371/journal.pone.0121322., eCollection 2015. PMID:25811865 doi:http://dx.doi.org/10.1371/journal.pone.0121322

1 Structural highlights
2 Publication Abstract from PubMed
3 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2lt1"

@@ Line 1: / Line 1: @@
 ==Solution NMR structure of the 72-residue N-terminal domain of Myxococcus xanthus CarD==
 <StructureSection load='2lt1' size='340' side='right' caption='[[2lt1]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
@@ Line 4: / Line 5: @@
 <table><tr><td colspan='2'>[[2lt1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_25232 Atcc 25232]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LT1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LT1 FirstGlance]. <br>
 </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">carD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=34 ATCC 25232])</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=2lt1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lt1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2lt1 RCSB], [http://www.ebi.ac.uk/pdbsum/2lt1 PDBsum]</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=2lt1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lt1 OCA], [http://pdbe.org/2lt1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2lt1 RCSB], [http://www.ebi.ac.uk/pdbsum/2lt1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2lt1 ProSAT]</span></td></tr>
 </table>
 <div style="background-color:#fffaf0;">
@@ Line 14: / Line 15: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2lt1" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

2lt1

From Proteopedia

Revision as of 17:22, 18 January 2017

Solution NMR structure of the 72-residue N-terminal domain of Myxococcus xanthus CarD

Structural highlights

Publication Abstract from PubMed

References

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Proteopedia Page Contributors and Editors (what is this?)

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