2L7I
The solution structure of the HAMP domain of the hypothetical transmembrane receptor Af1503 (A291F variant)
Summary for 2L7I
| Entry DOI | 10.2210/pdb2l7i/pdb |
| Related | 2ASW 2L7H 2y0q 2y0t 2y20 2y21 |
| Descriptor | Uncharacterized protein (1 entity in total) |
| Functional Keywords | signaling protein |
| Biological source | Archaeoglobus fulgidus |
| Total number of polymer chains | 2 |
| Total formula weight | 12994.84 |
| Authors | Coles, M.,Hulko, M.,Martin, J.,Lupas, A.N. (deposition date: 2010-12-09, release date: 2011-01-19, Last modification date: 2024-05-15) |
| Primary citation | Ferris, H.U.,Dunin-Horkawicz, S.,Mondejar, L.G.,Hulko, M.,Hantke, K.,Martin, J.,Schultz, J.E.,Zeth, K.,Lupas, A.N.,Coles, M. The Mechanisms of HAMP-Mediated Signaling in Transmembrane Receptors. Structure, 19:378-385, 2011 Cited by PubMed Abstract: 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. PubMed: 21397188DOI: 10.1016/j.str.2011.01.006 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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