TAILIEUCHUNG - Structure of quinoprotein methylamine dehydrogenase at 0 2.25 A resolution
The active site is located in a channel at the interface region between the H and L subunits, and the electron density in this part of the molecule suggests that the co-factor of this enzyme is not pyrrolo quinoline quinone (PQQ) itself, but might be instead a precursor of PQQ. | The EMBO Journal -2178, 1989 Structure of quinoprotein methylamine dehydrogenase at 0 A resolution , , , , Jzn.', , , , and Laboratory of Chemical Physics, University of Groningen, Nijenborgh 16, 9747 AG Groningen, 'Department of Microbiology and Enzymology, Delft University of Technology, Julianalaan 67, 2628 BC Delft, The Netherlands and 2EMBL Outstation, c/o DESY, Notkestrasse 85, 2000 Hamburg 52, FRG Communicated by The three-dimensional structure of quinoprotein methylamine dehydrogenase from Thiobacillus versutus has been determined at A resolution by a combination of multiple isomorphous replacement, phase extension by solvent flattening and partial structure phasing using molecular dynamics refinement. In the resulting map, the polypeptide chain for both subunits could be followed and an X-ray sequence was established. The tetrameric enzyme, made up of two heavy (H) and two light (L) subunits, is a flat parallelepiped with overall dimensions of -76 x 61 x 45 A. The H subunit, comprising 370 residues, is made up of two distinct segments: the first 31 residues form an extension which embraces one of the L subunits; the remaining residues are found in a disc-shaped domain. This domain is formed by a circular arrangement of seven topologically identical fourstranded antiparallel f-sheets, with 7-fold symmetry. In spite of distinct differences, this arrangement is reminiscent of the structure found in influenza virus neuraminidase. The L subunit consists of 121 residues, out of which 53 form a fl-sheet scaffold of a central three-stranded antiparallel sheet flanked by two shorter two-stranded antiparallel sheets. The remaining residues are found in segments of irregular structure. This subunit is stabilized by six disulphide bridges, plus two covalent bridges involving the quinone co-factor and residues 57 and 107 of
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