9hrk | pdb_00009hrk

Cytochrome P460 from Methyloccocus capsulatus in the ferrous state (single crosslink from Lys)

spinqualitylabelsall models 9hrk, resolution 1.33Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9hrk is a 2 chain structure with sequence from Methylococcus capsulatus str. Bath. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.33Å Ligands: HEC, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function G1UBD9_METCA Publication Abstract from PubMed Cytochromes P460 oxidise hydroxylamine within the nitrogen cycle and contain as their active site an unusual catalytic c-type haem where the porphyrin is crosslinked to the protein via a lysine residue in addition to the canonical cross links from cysteine residues. Understanding how enzymes containing P460 haem oxidise hydroxylamine into either nitrous oxide or nitric oxide has implications for climate change. Interestingly the P460-containing hydroxylamine oxidoreductase utilises a tyrosine crosslink to haem and performs similar chemistry. Previous crystal structures of cytochrome P460 from Nitrosomonas europaea (NeP460) clearly show the existence of a single crosslink between the NZ atom of lysine and the haem porphyrin, with mutagenesis studies indicating roles for the crosslink in positioning a proton transfer residue and/or influencing the distortion of the haem. Here we describe the evidence for a novel double crosslink between lysine and haem in the cytochrome P460 from Methylococcus capsulatus (Bath). In order to understand the complexities of this enzyme system we applied high resolution structural biology approaches at synchrotron and XFEL sources paired with crystal spectroscopies. Linked to this, we carried out QM/MM simulations that enabled the prediction of electronic absorption spectra providing a crucial validation to linking simulations and experimental structures. Our work demonstrates the feasibility of a double crosslink in McP460 and provides an opportunity to investigate how simulations can interact with experimental structures. Double crossed? Structural and computational studies of an unusually crosslinked haem in Methylococcus capsulatus cytochrome P460.,Pfalzgraf HE, Rao AG, Sen K, Adams HR, Edwards M, Lu Y, Yong C, Jaho S, Tosha T, Sugimoto H, Horrell S, Beilsten-Edmands J, Owen RL, Andrew CR, Worrall JAR, Tews I, Mulholland AJ, Hough MA, Keal TW Chem Sci. 2025 Aug 8. doi: 10.1039/d5sc04213e. PMID:40822104 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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