2lfr: Difference between revisions
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<StructureSection load='2lfr' size='340' side='right' caption='[[2lfr]], [[NMR_Ensembles_of_Models | 18 NMR models]]' scene=''> | <StructureSection load='2lfr' size='340' side='right' caption='[[2lfr]], [[NMR_Ensembles_of_Models | 18 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
[[2lfr]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arcfu Arcfu]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LFR OCA]. <br> | <table><tr><td colspan='2'>[[2lfr]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arcfu Arcfu]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LFR OCA]. <br> | ||
<b>[[Related_structure|Related:]]</b> [[3zrx|3zrx]], [[3zrw|3zrw]], [[3zrv|3zrv]], [[2lfs|2lfs]]< | </td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3zrx|3zrx]], [[3zrw|3zrw]], [[3zrv|3zrv]], [[2lfs|2lfs]]</td></tr> | ||
<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>[[Gene|Gene:]]</b></td><td class="sblockDat">AF_1503 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224325 ARCFU])</td></tr> | ||
<b>Resources:</b> <span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2lfr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lfr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2lfr RCSB], [http://www.ebi.ac.uk/pdbsum/2lfr PDBsum]</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> | ||
<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=2lfr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lfr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2lfr RCSB], [http://www.ebi.ac.uk/pdbsum/2lfr PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Bacterial transmembrane receptors regulate an intracellular catalytic output in response to extracellular sensory input. To investigate the conformational changes that relay the regulatory signal, we have studied the HAMP domain, a ubiquitous intracellular module connecting input to output domains. HAMP forms a parallel, dimeric, four-helical coiled coil, and rational substitutions in our model domain (Af1503 HAMP) induce a transition in its interhelical packing, characterized by axial rotation of all four helices (the gearbox signaling model). We now illustrate how these conformational changes are propagated to a downstream domain by fusing Af1503 HAMP variants to the DHp domain of EnvZ, a bacterial histidine kinase. Structures of wild-type and mutant constructs are correlated with ligand response in vivo, clearly associating them with distinct signaling states. We propose that altered recognition of the catalytic domain by DHp, rather than a shift in position of the phospho-accepting histidine, forms the basis for regulation of kinase activity. | Bacterial transmembrane receptors regulate an intracellular catalytic output in response to extracellular sensory input. To investigate the conformational changes that relay the regulatory signal, we have studied the HAMP domain, a ubiquitous intracellular module connecting input to output domains. HAMP forms a parallel, dimeric, four-helical coiled coil, and rational substitutions in our model domain (Af1503 HAMP) induce a transition in its interhelical packing, characterized by axial rotation of all four helices (the gearbox signaling model). We now illustrate how these conformational changes are propagated to a downstream domain by fusing Af1503 HAMP variants to the DHp domain of EnvZ, a bacterial histidine kinase. Structures of wild-type and mutant constructs are correlated with ligand response in vivo, clearly associating them with distinct signaling states. We propose that altered recognition of the catalytic domain by DHp, rather than a shift in position of the phospho-accepting histidine, forms the basis for regulation of kinase activity. | ||
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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/> | ||