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Closely spaced acidic residues that coordinate divalent cations are characteristic of the active sites of most nucleic acid polymerases, in spite of the fact that they belong to several unrelated structural folds [ 9 13 14 17 28 29 59 ] . Given that the DbDGD motif is the only set of closely spaced acidic residues shared by the RDRPs and the YRHs, it is likely to form part of the nucleotidyltransferase active site of these enzymes.
A DALI search [ 20] of the PDB database with this β-barrel revealed no specific structural relationships with other folds such as the OB fold or the SH3-like barrel beyond the presence of curved β-sheets, suggesting that it represents a domain with a distinct fold (Figure 2).
The opsonization activity of PMNs was increased 6-8 folds by prior incubation with monoclonal antibodies.
At high magnification, the surface topography of the EN fibers is easily visualized, facilitating quantification of the membrane fiber folds of the cell surfaces (Fig.
folds