6j1i

Crystal structure of HypX from Aquifex aeolicus, A392F-I419F variant

spinqualitylabelsall models 6j1i, resolution 2.29Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6j1i is a 1 chain structure with sequence from Aquifex aeolicus VF5. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.29Å Ligands: COA, GOL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function O67224_AQUAE Publication Abstract from PubMed Several accessory proteins are required for the assembly of the metal centers in hydrogenases. In NiFe-hydrogenases, CO and CN(-) are coordinated to the Fe in the NiFe dinuclear cluster of the active center. Though these diatomic ligands are biosynthesized enzymatically, detail mechanisms of their biosynthesis remain unclear. Here, we report the structural characterization of HypX responsible for CO biosynthesis to assemble the active site of NiFe hydrogenase. CoA is constitutionally bound in HypX. Structural characterization of HypX suggests that the formyl-group transfer will take place from N(10)-formyl-THF to CoA to form formyl-CoA in the N-terminal domain of HypX, followed by decarbonylation of formyl-CoA to produce CO in the C-terminal domain though the direct experimental results are not available yet. The conformation of CoA accommodated in the continuous cavity connecting the N- and C-terminal domains will interconvert between the extended and the folded conformations for HypX catalysis. Structural characterization of HypX responsible for CO biosynthesis in the maturation of NiFe-hydrogenase.,Muraki N, Ishii K, Uchiyama S, Itoh SG, Okumura H, Aono S Commun Biol. 2019 Oct 18;2:385. doi: 10.1038/s42003-019-0631-z. eCollection 2019. PMID:31646188 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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