1xj3 | pdb_00001xj3

bjFixLH in unliganded ferrous form

spinqualitylabelsall models 1xj3, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1xj3 is a 1 chain structure with sequence from "rhizobacterium_japonicum"_kirchner_1896 "rhizobacterium japonicum" kirchner 1896. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: HEM Related: 1xj2, 1xj4, 1xj6 Gene: fixL ("Rhizobacterium japonicum" Kirchner 1896) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [FIXL_BRAJA] Putative oxygen sensor; modulates the activity of FixJ, a transcriptional activator of nitrogen fixation fixK gene. FixL probably acts as a kinase that phosphorylates FixJ. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Rhizobia directly regulate the expression of genes required for symbiotic nitrogen fixation in response to oxygen concentration via the sensor protein FixL. The N-terminal PAS domain of FixL contains a histidine-coordinated heme and regulates the activity of its effector domain, a C-terminal histidine kinase, in response to binding of oxygen and other ligands at the heme. To further investigate ligand-induced inhibition of FixL, we have determined the crystal structures of the heme domain in both the deoxy state and bound to carbon monoxide, a weak inhibitor of FixL kinase activity. Structures collected at room temperature are presented in each state from two crystallographic space groups at 1.8 and 2 A resolution. These structures reveal displacement of the residues of the H(beta) and I(beta) strands by Leu236 upon CO binding, and this structural change propagates more than 15 A to a region of the structure implicated in signal transduction in PAS proteins. Displacement of residues Ile215, Ile216, and Gly217 in the FG loop is also evident, accompanied by the movement of heme propionate 6 upon change in iron ligation. CO binding increases the temperature factors in the FG loop of the protein and disorders the side chain of Arg206, a conserved residue involved in the FG loop switch mechanism. We relate these results to structural changes in other PAS sensor domains and their involvement in catalytic control. Crystal structures of deoxy and CO-bound bjFixLH reveal details of ligand recognition and signaling.,Key J, Moffat K Biochemistry. 2005 Mar 29;44(12):4627-35. PMID:15779889 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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