2e7z

Acetylene Hydratase from Pelobacter acetylenicus

spinqualitylabelsall models 2e7z, resolution 1.26Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2e7z is a 1 chain structure with sequence from Syntrophotalea acetylenica. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.26Å Ligands: ACT, MGD, MPD, NA, W Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function AHY_SYNAC Catalyzes the hydration of acetylene to form acetaldehyde. Ethylene cannot act as a substrate. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The tungsten-iron-sulfur enzyme acetylene hydratase stands out from its class because it catalyzes a nonredox reaction, the hydration of acetylene to acetaldehyde. Sequence comparisons group the protein into the dimethyl sulfoxide reductase family, and it contains a bis-molybdopterin guanine dinucleotide-ligated tungsten atom and a cubane-type [4Fe:4S] cluster. The crystal structure of acetylene hydratase at 1.26 A now shows that the tungsten center binds a water molecule that is activated by an adjacent aspartate residue, enabling it to attack acetylene bound in a distinct, hydrophobic pocket. This mechanism requires a strong shift of pK(a) of the aspartate, caused by a nearby low-potential [4Fe:4S] cluster. To access this previously unrecognized W-Asp active site, the protein evolved a new substrate channel distant from where it is found in other molybdenum and tungsten enzymes. Structure of the non-redox-active tungsten/[4Fe:4S] enzyme acetylene hydratase.,Seiffert GB, Ullmann GM, Messerschmidt A, Schink B, Kroneck PM, Einsle O Proc Natl Acad Sci U S A. 2007 Feb 27;104(9):3073-7. PMID:17360611 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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