6ttl | pdb_00006ttl

crystal structure of [FeFe]-hydrogenase CbA5H (partial) from Clostridium beijerinckii in Hinact state

spinqualitylabelsall models 6ttl, resolution 2.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6ttl is a 2 chain structure with sequence from Clostridium beijerinckii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.9Å Ligands: 402, SF4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A1I9RYV3_CLOBE Publication Abstract from PubMed [FeFe]-hydrogenases are efficient H(2)-catalysts, yet upon contact with dioxygen their catalytic cofactor (H-cluster) is irreversibly inactivated. Here, we combine X-ray crystallography, rational protein design, direct electrochemistry, and Fourier-transform infrared spectroscopy to describe a protein morphing mechanism that controls the reversible transition between the catalytic H(ox)-state and the inactive but oxygen-resistant H(inact)-state in [FeFe]-hydrogenase CbA5H of Clostridium beijerinckii. The X-ray structure of air-exposed CbA5H reveals that a conserved cysteine residue in the local environment of the active site (H-cluster) directly coordinates the substrate-binding site, providing a safety cap that prevents O(2)-binding and consequently, cofactor degradation. This protection mechanism depends on three non-conserved amino acids situated approximately 13 A away from the H-cluster, demonstrating that the 1st coordination sphere chemistry of the H-cluster can be remote-controlled by distant residues. A safety cap protects hydrogenase from oxygen attack.,Winkler M, Duan J, Rutz A, Felbek C, Scholtysek L, Lampret O, Jaenecke J, Apfel UP, Gilardi G, Valetti F, Fourmond V, Hofmann E, Leger C, Happe T Nat Commun. 2021 Feb 2;12(1):756. doi: 10.1038/s41467-020-20861-2. PMID:33531463 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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