2E7Z

Acetylene Hydratase from Pelobacter acetylenicus

Summary for 2E7Z

• Entry DOI: 10.2210/pdb2e7z/pdb
• Descriptor: Acetylene hydratase Ahy, SODIUM ION, ACETATE ION, ... (8 entities in total)
• Functional Keywords: tungstoprotein, dmso reductase family, iron-sulfur-cluster, lyase
• Biological source: Pelobacter acetylenicus
• Total number of polymer chains: 1
• Total formula weight: 83985.80

Authors

Einsle, O.,Kroneck, P.M.H.,Seiffert, G.B.,Messerschmidt, A. (deposition date: 2007-01-15, release date: 2007-02-27, Last modification date: 2019-09-04)

Primary citation

Seiffert, G.B.,Ullmann, G.M.,Messerschmidt, A.,Schink, B.,Kroneck, P.M.H.,Einsle, O.
Structure of the non-redox-active tungsten/[4Fe:4S] enzyme acetylene hydratase
Proc.Natl.Acad.Sci.Usa, 104:3073-3077, 2007

PubMed Abstract: 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.

PubMed: 17360611
DOI: 10.1073/pnas.0610407104

Experimental method

X-RAY DIFFRACTION (1.26 Å)