3ZRX
The high resolution structure of a dimeric Hamp-Dhp fusion displays strong asymmetry
Summary for 3ZRX
| Entry DOI | 10.2210/pdb3zrx/pdb |
| Related | 1BXD 1JOY 1NJV 2Y0Q 2Y0T 2Y20 2Y21 3ZRV 3ZRW |
| Descriptor | AF1503 PROTEIN, OSMOLARITY SENSOR PROTEIN ENVZ (2 entities in total) |
| Functional Keywords | signaling protein, osmoregulation, ompr, ompc |
| Biological source | ARCHAEOGLOBUS FULGIDUS More |
| Cellular location | Cell inner membrane; Multi-pass membrane protein: P0AEJ4 |
| Total number of polymer chains | 2 |
| Total formula weight | 26167.69 |
| Authors | Zeth, K.,Hulko, M.,Martin, J. (deposition date: 2011-06-20, release date: 2011-06-29, Last modification date: 2023-12-20) |
| Primary citation | Ferris, H.U.,Dunin-Horkawicz, S.,Hornig, N.,Hulko, M.,Martin, J.,Schultz, J.E.,Zeth, K.,Lupas, A.N.,Coles, M. Mechanism of Regulation of Receptor Histidine Kinases. Structure, 20:56-, 2012 Cited by PubMed Abstract: 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. PubMed: 22244755DOI: 10.1016/J.STR.2011.11.014 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.25 Å) |
Structure validation
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