8cns

The Hybrid Cluster Protein from the thermophilic methanogen Methanothermococcus thermolithotrophicus in a mixed redox state after soaking with hydroxylamine, at 1.36-A resolution.

spinqualitylabelsall models 8cns, resolution 1.36Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8cns is a 1 chain structure with sequence from Methanothermococcus thermolithotrophicus DSM 2095. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.36Å Ligands: ACT, CSS, EDO, FMT, GOL, HOA, MG, MRD, PEG, PG5, SF3, TRS Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Whilst widespread in the microbial world, the hybrid cluster protein (HCP) has been paradoxically a long-time riddle for microbiologists. During three decades, numerous studies on a few model organisms unravelled its structure and dissected its metal-containing catalyst, but the physiological function of the enzyme remained elusive. Recent studies on bacteria point towards a nitric oxide reductase activity involved in resistance during nitrate and nitrite reduction as well as host infection. In this study, we isolated and characterised a naturally highly produced HCP class I from a marine methanogenic archaeon grown on ammonia. The crystal structures of the enzyme in a reduced and partially oxidised state, obtained at a resolution of 1.45 and 1.36-A, respectively, offered a precise picture of the archaeal enzyme intimacy. There are striking similarities with the well-studied enzymes from Desulfovibrio species regarding sequence, kinetic parameters, structure, catalyst conformations, and internal channelling systems. The close phylogenetic relationship between the enzymes from Methanococcales and many Bacteria corroborates this similarity. Indeed, Methanococcales HCPs are closer to these bacterial homologues than to any other archaeal enzymes. The relatively high constitutive production of HCP in M. thermolithotrophicus, in the absence of a notable nitric oxide source, questions the physiological function of the enzyme in these ancient anaerobes. Structural and biochemical elucidation of class I hybrid cluster protein natively extracted from a marine methanogenic archaeon.,Lemaire ON, Belhamri M, Wagner T Front Microbiol. 2023 May 11;14:1179204. doi: 10.3389/fmicb.2023.1179204. , eCollection 2023. PMID:37250035 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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