6za1

Structure of [NiFeSe] hydrogenase G491A variant from Desulfovibrio vulgaris Hildenborough pressurized with Oxygen gas - structure G491A-O2-hd

spinqualitylabelsall models 6za1, resolution 1.37Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6za1 is a 2 chain structure with sequence from Desulfovibrio vulgaris str. Hildenborough. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.37Å Ligands: CSD, FCO, FE2, GOL, H2S, NI, OXY Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q72AS4_NITV2 Publication Abstract from PubMed Hydrogenases are metalloenzymes that catalyse both H2 evolution and uptake. They are gas-processing enzymes with deeply buried active sites, so the gases diffuse through channels that connect the active site to the protein surface. The [NiFeSe] hydrogenases are a special class of hydrogenases containing a selenocysteine as a nickel ligand; they are more catalytically active and less O2-sensitive than standard [NiFe] hydrogenases. Characterisation of the channel system of hydrogenases is important to understand how the inhibitor oxygen reaches the active site to cause oxidative damage. To this end, crystals of Desulfovibrio vulgaris Hildenborough [NiFeSe] hydrogenase were pressurized with krypton and oxygen, and a method for tracking labile O2 molecules was developed, for mapping a hydrophobic channel system similar to that of the [NiFe] enzymes as the major route for gas diffusion. Exploring the gas access routes in a [NiFeSe] hydrogenase using crystals pressurized with krypton and oxygen.,Zacarias S, Temporao A, Carpentier P, van der Linden P, Pereira IAC, Matias PM J Biol Inorg Chem. 2020 Aug 31. pii: 10.1007/s00775-020-01814-y. doi:, 10.1007/s00775-020-01814-y. PMID:32865640 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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