4cxf

From Proteopedia

(Difference between revisions)

Revision as of 05:31, 5 August 2016

Structure of CnrH in complex with the cytosolic domain of CnrY.

Structural highlights

4cxf is a 2 chain structure with sequence from Cupriavidus metallidurans ch34. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CNRH_RALME] Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor regulates the genes for a membrane-located efflux system that confers resistance to nickel and cobalt. CnrH alone is able to activate CNR expression, while both CnrY and CrnX are needed for nickel induction of cnrH (PubMed:10671463). Binds DNA in an RNA polymerase-dependent fashion (PubMed:10671464). CnrH may be controlled by a CnrYX transmembrane anti-sigma factor complex which binds CnrH in the absence of Ni(2+). If Ni(2+) appears in the periplasm, it may be bound by CnrR (CnrX); the signal then would be transmitted by CnrY into the cytoplasm and CnrH would be released. [CNRY_RALME] Nickel and cobalt resistance proteins CnrA, CnrB, CnrC CnrH and CnrR may be involved in the regulation of CNR. CnrH alone is able to activate cnr expression, and both CnrY and CrnX are needed for nickel induction of CnrH (PubMed:10671463). In the absence of wild-type CnrY (due either to a frameshift, PubMed:10671463 or absence of the transcript, PubMed:10671464), nickel and cobalt resistance is constitutive, indicating that CrnY may act as a repressor (PubMed:10671463) or an anti-sigma factor (PubMed:10671464).

Publication Abstract from PubMed

Gene expression in bacteria is regulated at the level of transcription initiation, a process driven by sigma factors. The regulation of sigma factor activity proceeds from the regulation of their cytoplasmic availability, which relies on specific inhibitory proteins called anti-sigma factors. With anti-sigma factors regulating their availability according to diverse cues, extracytoplasmic function sigma factors (sigmaECF) form a major signal transduction system in bacteria. Here, structure:function relationships have been characterized in an emerging class of minimal-size transmembrane anti-sigma factors, using CnrY from Cupriavidus metallidurans CH34 as a model. This study reports the 1.75-A-resolution structure of CnrY cytosolic domain in complex with CnrH, its cognate sigmaECF, and identifies a small hydrophobic knob in CnrY as the major determinant of this interaction in vivo. Unsuspected structural similarity with the molecular switch regulating the general stress response in alpha-proteobacteria unravels a new class of anti-sigma factors targeting sigmaECF. Members of this class carry out their function via a 30-residue stretch that displays helical propensity but no canonical structure on its own.

The Crystal Structure of the Anti-sigma Factor CnrY in Complex with the sigma Factor CnrH Shows a New Structural Class of Anti-sigma Factors Targeting Extracytoplasmic Function sigma Factors.,Maillard AP, Girard E, Ziani W, Petit-Hartlein I, Kahn R, Coves J J Mol Biol. 2014 Apr 12. pii: S0022-2836(14)00177-6. doi:, 10.1016/j.jmb.2014.04.003. PMID:24727125^[1]

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

References

↑ Maillard AP, Girard E, Ziani W, Petit-Hartlein I, Kahn R, Coves J. The Crystal Structure of the Anti-sigma Factor CnrY in Complex with the sigma Factor CnrH Shows a New Structural Class of Anti-sigma Factors Targeting Extracytoplasmic Function sigma Factors. J Mol Biol. 2014 Apr 12. pii: S0022-2836(14)00177-6. doi:, 10.1016/j.jmb.2014.04.003. PMID:24727125 doi:http://dx.doi.org/10.1016/j.jmb.2014.04.003

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4cxf"

@@ Line 1: / Line 1: @@
 ==Structure of CnrH in complex with the cytosolic domain of CnrY.==
 <StructureSection load='4cxf' size='340' side='right' caption='[[4cxf]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
@@ Line 4: / Line 5: @@
 <table><tr><td colspan='2'>[[4cxf]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Cupriavidus_metallidurans_ch34 Cupriavidus metallidurans ch34]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CXF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CXF FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=4cxf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cxf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cxf RCSB], [http://www.ebi.ac.uk/pdbsum/4cxf 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=4cxf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cxf OCA], [http://pdbe.org/4cxf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4cxf RCSB], [http://www.ebi.ac.uk/pdbsum/4cxf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4cxf ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 16: / Line 17: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4cxf" style="background-color:#fffaf0;"></div>
 ==See Also==

4cxf

From Proteopedia

Revision as of 05:31, 5 August 2016

Structure of CnrH in complex with the cytosolic domain of CnrY.

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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