4cxf
From Proteopedia
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- | ''' | + | ==Structure of CnrH in complex with the cytosolic domain of CnrY.== |
+ | <StructureSection load='4cxf' size='340' side='right' caption='[[4cxf]], [[Resolution|resolution]] 1.75Å' 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 | + | 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> |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | == References == | |
- | + | <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]] |
Revision as of 07:49, 30 April 2014
Structure of CnrH in complex with the cytosolic domain of CnrY.
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