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4cxf
From Proteopedia
(Difference between revisions)
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<StructureSection load='4cxf' size='340' side='right' caption='[[4cxf]], [[Resolution|resolution]] 1.75Å' scene=''> | <StructureSection load='4cxf' size='340' side='right' caption='[[4cxf]], [[Resolution|resolution]] 1.75Å' scene=''> | ||
== Structural highlights == | == 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> | + | <table><tr><td colspan='2'>[[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>[[Ligand|Ligands:]]</b> <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br> | + | </td></tr><tr><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><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>< | + | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr> |
| - | <b>Resources:</b> <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>< | + | <tr><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> |
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == 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. | 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. | ||
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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> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 09:25, 1 May 2014
Structure of CnrH in complex with the cytosolic domain of CnrY.
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