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at 1.72 A resolution. The s-GDH monomer has a beta-propeller fold consisting of six four-stranded anti-parallel beta-sheets aligned around a pseudo 6-fold symmetry axis. The enzyme binds three calcium ions per monomer, two of which are located in the dimer interface. The third is bound in the putative active site, where it may bind and functionalize the pyrroloquinoline quinone cofactor
strucuture of soluble isoform sGDH with the cofactor at 2.2 A resolution, and of its complex with reduced cofactor and D-glucose at 1.9 A resolution. Evidence for a mechanism comprisding general base-catalyzed hydride transfer
ternary complex of s-GDH with PQQ and methylhydrazine, at 1.5 A resolution. Formation of a covalent PQQ adduct in the active-site. The C5 carbonyl group of the cofactor is the most reactive moiety of PQQ. The binding of the cofactor to s-GDH is predominantly governed by polar interactions. The C2, C7, and C9 carboxyl groups of PQQ form salt bridges with Arg408, Lys377, and Arg406, respectively. The ortho-quinone O4 and O5 atoms are bound by Asn229 and Arg228, respectively. The N6, O7A, and O5 atoms of PQQ are ligands for the active-site calcium ion. The other calcium ligands are provided by the two main chain carbonyl oxygen atoms of Gly-247 and Pro-248 and two watermolecules