2y0q: Difference between revisions
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<StructureSection load='2y0q' size='340' side='right'caption='[[2y0q]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='2y0q' size='340' side='right'caption='[[2y0q]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2y0q]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2y0q]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Arcfl Arcfl]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Y0Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Y0Q FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2y20|2y20]], [[2y21|2y21]], [[2y0t|2y0t]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2y20|2y20]], [[2y21|2y21]], [[2y0t|2y0t]]</div></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2y0q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y0q OCA], [https://pdbe.org/2y0q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2y0q RCSB], [https://www.ebi.ac.uk/pdbsum/2y0q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2y0q ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
Revision as of 15:21, 27 April 2022
The mechanisms of HAMP-mediated signaling in transmembrane receptors - the A291C mutantThe mechanisms of HAMP-mediated signaling in transmembrane receptors - the A291C mutant
Structural highlights
Publication Abstract from PubMedHAMP domains mediate signal transduction in over 7500 enzyme-coupled receptors represented in all kingdoms of life. The HAMP domain of the putative archaeal receptor Af1503 has a parallel, dimeric, four-helical coiled coil structure, but with unusual core packing, related to canonical packing by concerted axial rotation of the helices. This has led to the gearbox model for signal transduction, whereby the alternate packing modes correspond to signaling states. Here we present structures of a series of Af1503 HAMP variants. We show that substitution of a conserved small side chain within the domain core (A291) for larger residues induces a gradual transition in packing mode, involving both changes in helix rotation and bundle shape, which are most prominent at the C-terminal, output end of the domain. These are correlated with activity and ligand response in vitro and in vivo by incorporating Af1503 HAMP into mycobacterial adenylyl cyclase assay systems. The Mechanisms of HAMP-Mediated Signaling in Transmembrane Receptors.,Ferris HU, Dunin-Horkawicz S, Mondejar LG, Hulko M, Hantke K, Martin J, Schultz JE, Zeth K, Lupas AN, Coles M Structure. 2011 Mar 9;19(3):378-85. PMID:21397188[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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