6tv2 | pdb_00006tv2

Heme d1 biosynthesis associated Protein NirF

spinqualitylabelsall models 6tv2, resolution 1.56Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6tv2 is a 8 chain structure with sequence from Pseae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GOL, MPO, SO4 Gene: nirF, PA0516 (PSEAE) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [NIRF_PSEAE] Required for the biosynthesis of heme d1 of nitrite reductase. Could have a dehydrogenase activity yielding sirohydrochlorin from precorrin-2 or dehydrogenation of propionate side chain C17. Publication Abstract from PubMed Certain facultative anaerobes such as the opportunistic human pathogen Pseudomonas aeruginosa can respire on nitrate, a process generally known as denitrification. This enables denitrifying bacteria to survive in anoxic environments and contributes e.g. to the formation of biofilm, hence increasing difficulties in eradicating P. aeruginosa infections. A central step in denitrification is the reduction of nitrite to nitric oxide by nitrite reductase NirS, an enzyme that requires the unique cofactor heme d1 . While heme d1 biosynthesis is mostly understood, the role of the essential periplasmatic protein NirF in this pathway remains unclear. Here, we have determined crystal structures of NirF and its complex with dihydroheme d1 , the last intermediate of heme d1 biosynthesis. We found that NirF forms a bottom-to-bottom beta-propeller homodimer and confirmed this by multi-angle light and small-angle X-ray scattering. The N-termini are adjacent to each other and project away from the core structure, which hints at simultaneous membrane anchoring via both N-termini. Further, the complex with dihydroheme d1 allowed us to probe the importance of specific residues in the vicinity of the ligand binding site, revealing residues not required for binding or stability of NirF but essential for denitrification in experiments with complemented mutants of a DeltanirF strain of P. aeruginosa. Together, these data suggest that NirF possesses a yet unknown enzymatic activity and is not simply a binding protein of heme d1 derivatives. Crystal structure of NirF: Insights into its role in heme d1 biosynthesis.,Klunemann T, Nimtz M, Jansch L, Layer G, Blankenfeldt W FEBS J. 2020 Apr 7. doi: 10.1111/febs.15323. PMID:32255259 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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