5ohf

Globin sensor domain of AfGcHK (FeIII form) in complex with cyanide, partially reduced

spinqualitylabelsall models 5ohf, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5ohf is a 8 chain structure with sequence from Anaeromyxobacter sp. Fw109-5. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.8Å Ligands: CL, CYN, HEM, NA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function GCHK_ANADF Member of the two-component regulatory system GcHK/Anae109_2439. Autophosphorylates in response to oxygen availability, and then transfers the phosphate group to a conserved Asp residue in the receiver domains of the cognate response regulator Anae109_2439, resulting in its activation. Publication Abstract from PubMed The heme-based oxygen sensor histidine kinase AfGcHK is part of a two-component signal transduction system in bacteria. O2 binding to the Fe(II) heme complex of its N-terminal globin domain strongly stimulates autophosphorylation at His-183 in its C-terminal kinase domain. The 6-coordinate heme Fe(III)-OH- and -CN- complexes of AfGcHK are also active, but the 5-coordinate heme Fe(II) complex and the heme-free apo-form are inactive. Here, we determined the crystal structures of the isolated dimeric globin domains of the active Fe(III)-CN- and inactive 5-coordinate Fe(II) forms, revealing striking structural differences on the heme-proximal side of the globin domain. Using hydrogen/deuterium exchange coupled with mass spectrometry (HDX-MS) to characterize the conformations of the active and inactive forms of full-length AfGcHK in solution, we investigated the intramolecular signal transduction mechanisms. Major differences between the active and inactive forms were observed on the heme-proximal side (helix H5), at the dimerization interface (helices H6, H7, and loop L7) of the globin domain, and in the ATP-binding site (helices H9 and H11) of the kinase domain. Moreover, separation of the sensor and kinase domains, which deactivates catalysis, increased the solvent exposure of the globin domain-dimerization interface (helix H6) as well as the flexibility and solvent exposure of helix H11. Together, these results suggest that structural changes at the heme proximal side, the globin domain-dimerization interface, and the ATP-binding site are important in the signal transduction mechanism of AfGcHK. We conclude that AfGcHK functions as an ensemble of molecules sampling at least two conformational states. Coordination and redox state-dependent structural changes of the heme-based oxygen sensor AfGcHK associated with intraprotein signal transduction.,Stranava M, Man P, Skalova T, Kolenko P, Blaha J, Fojtikova V, Martinek V, Dohnalek J, Lengalova A, Rosulek M, Shimizu T, Martinkova M J Biol Chem. 2017 Nov 1. pii: jbc.M117.817023. doi: 10.1074/jbc.M117.817023. PMID:29092908 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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