2e7z

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Revision as of 17:17, 29 January 2008

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spinqualitylabelsall models 2e7z, resolution 1.26Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Acetylene Hydratase from Pelobacter acetylenicus

Overview

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.

About this Structure

2E7Z is a Single protein structure of sequence from Pelobacter acetylenicus with , , , , and as ligands. Active as Deleted entry, with EC number 4.2.1.71 Full crystallographic information is available from OCA.

Reference

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

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