2y21: Difference between revisions
New page: '''Unreleased structure''' The entry 2y21 is ON HOLD Authors: Zeth, K., Ferris, H.U., Hulko, M., Lupas, A.N. Description: The mechanisms of HAMP-mediated signaling in transmembrane rec... |
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The | ==The mechanisms of HAMP-mediated signaling in transmembrane receptors - the A291V mutant== | ||
<StructureSection load='2y21' size='340' side='right'caption='[[2y21]], [[Resolution|resolution]] 2.45Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2y21]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Y21 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Y21 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.45Å</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2y21 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y21 OCA], [https://pdbe.org/2y21 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2y21 RCSB], [https://www.ebi.ac.uk/pdbsum/2y21 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2y21 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/O28769_ARCFU O28769_ARCFU] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
HAMP 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<ref>PMID:21397188</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2y21" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Archaeoglobus fulgidus]] | |||
[[Category: Large Structures]] | |||
[[Category: Ferris HU]] | |||
[[Category: Hulko M]] | |||
[[Category: Lupas AN]] | |||
[[Category: Zeth K]] | |||
Latest revision as of 18:45, 4 October 2023
The mechanisms of HAMP-mediated signaling in transmembrane receptors - the A291V mutantThe mechanisms of HAMP-mediated signaling in transmembrane receptors - the A291V mutant
Structural highlights
FunctionPublication 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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