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| | ==The solution structure of the HAMP domain of the hypothetical transmembrane receptor Af1503== | | ==The solution structure of the HAMP domain of the hypothetical transmembrane receptor Af1503== |
| - | <StructureSection load='2l7h' size='340' side='right' caption='[[2l7h]], [[NMR_Ensembles_of_Models | 18 NMR models]]' scene=''> | + | <StructureSection load='2l7h' size='340' side='right'caption='[[2l7h]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2l7h]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arcfl Arcfl]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2asw 2asw] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2asx 2asx]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L7H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2L7H FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2l7h]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2asw 2asw] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2asx 2asx]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L7H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L7H FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2asw|2asw]], [[2l7i|2l7i]], [[2y0q|2y0q]], [[2y0t|2y0t]], [[2y20|2y20]], [[2y21|2y21]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">af1503, AF_1503 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2234 ARCFL])</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=2l7h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l7h OCA], [https://pdbe.org/2l7h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l7h RCSB], [https://www.ebi.ac.uk/pdbsum/2l7h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l7h ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2l7h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l7h OCA], [http://pdbe.org/2l7h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2l7h RCSB], [http://www.ebi.ac.uk/pdbsum/2l7h PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/O28769_ARCFU O28769_ARCFU] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Arcfl]] | + | [[Category: Archaeoglobus fulgidus]] |
| - | [[Category: Coles, M]] | + | [[Category: Large Structures]] |
| - | [[Category: Hulko, M]] | + | [[Category: Coles M]] |
| - | [[Category: Lupas, A N]] | + | [[Category: Hulko M]] |
| - | [[Category: Martin, J]] | + | [[Category: Lupas AN]] |
| - | [[Category: Complementary x-da]] | + | [[Category: Martin J]] |
| - | [[Category: Signaling protein]]
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| Structural highlights
Function
O28769_ARCFU
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ferris HU, Dunin-Horkawicz S, Mondejar LG, Hulko M, Hantke K, Martin J, Schultz JE, Zeth K, Lupas AN, Coles M. The Mechanisms of HAMP-Mediated Signaling in Transmembrane Receptors. Structure. 2011 Mar 9;19(3):378-85. PMID:21397188 doi:10.1016/j.str.2011.01.006
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