5xdh

His/DOPA ligated cytochrome c from an anammox organism KSU-1

spinqualitylabelsall models 5xdh, resolution 1.32Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5xdh is a 4 chain structure with sequence from Candidatus Jettenia caeni. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.32Å Ligands: ACT, DAH, HEC, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function I3IL56_9BACT Publication Abstract from PubMed Anammox is a bacterial energy metabolic process that forms N2 gas from nitrite and ammonium ions. The enzymatic mechanisms of anammox have been gradually revealed; however, the electron transport chain in anammox bacteria remains poorly understood. In the present study, we purified and characterized two low-molecular-weight c-type cytochromes from an enriched culture of the anammox bacterium strain, KSU-1. Their genes, KSU1_B0428 and KSU1_C0855, were identified in the KSU-1 genome, and their recombinant proteins were characterized. KSU1_B0428 is a typical c-type cytochrome with a His/Met coordinated heme, acting as an electron transfer protein. In contrast, KSU1_C0855 could not be assigned as a known cytochrome and its heme was suggested to have an uncommon axial ligand set. Crystal structural analyses of C0855 clearly showed that its heme iron is coordinated by His15 as a fifth ligand. Moreover, the sixth coordination site is occupied by the aromatic ring of Tyr60, and an unassignable electron density that is inseparable with that of aromatic carbon of Tyr60 was found. The additional electron density was assigned to an O atom by molecular mass analyses. Therefore, Tyr60 would be chemically modified to 3,4-dihydroxyphenylalanine and bound to the Fe atom. We revealed that an anammox bacterium strain KSU-1 expresses a novel cytochrome c having an unprecedented His/3,4-dihydroxyphenylalanine coordinating heme. The expression of the novel c-type cytochrome might be required for the redox reaction of the anammox process. Anammox Organism KSU-1 Expresses a Novel His/DOPA Ligated Cytochrome c.,Hira D, Kitamura R, Nakamura T, Yamagata Y, Furukawa K, Fujii T J Mol Biol. 2018 Apr 13;430(8):1189-1200. doi: 10.1016/j.jmb.2018.02.017. Epub, 2018 Feb 23. PMID:29481839 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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