4cxf: Difference between revisions

Line 1:

'''~~Unreleased~~ structure'''

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

== Structural highlights ==

[[4cxf]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CXF OCA].

Activity: [http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2]

== 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 ~~entry 4cxf is ON HOLD until Paper Publication~~

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<ref>PMID:24727125</ref>

~~Authors: Maillard~~, A.P., Girard, E., ~~Ziani~~, W., Petit-Hartlein, I., ~~Kahn, R., Coves, J~~.

From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.

== References ==

~~Description~~: ~~Structure of CnrH in complex with the cytosolic domain of CnrY.~~

__TOC__

</StructureSection>

[[Category: Coves, J.]]

[[Category: Girard, E.]]

[[Category: Kahn, R.]]

[[Category: Maillard, A P.]]

[[Category: Petit-Hartlein, I.]]

[[Category: Ziani, W.]]

[[Category: Antisigma]]

[[Category: Ecf-type sigma]]

[[Category: Transcription]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+==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=''>
+== Structural highlights ==
+[[4cxf]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CXF OCA]. <br>
+<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>
+== 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 entry 4cxf is ON HOLD  until Paper Publication
+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<ref>PMID:24727125</ref>
-Authors: Maillard, A.P., Girard, E., Ziani, W., Petit-Hartlein, I., Kahn, R., Coves, J.
+From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
+== References ==
-Description: Structure of CnrH in complex with the cytosolic domain of CnrY.
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Coves, J.]]
+[[Category: Girard, E.]]
+[[Category: Kahn, R.]]
+[[Category: Maillard, A P.]]
+[[Category: Petit-Hartlein, I.]]
+[[Category: Ziani, W.]]
+[[Category: Antisigma]]
+[[Category: Ecf-type sigma]]
+[[Category: Transcription]]