Article ID Journal Published Year Pages File Type
10761828 Biochemical and Biophysical Research Communications 2012 6 Pages PDF
Abstract
► We solve structures of Bsp165PelA in apo-form and in complex with trigalacturonate. ► Parallel β-helix motif, substrate binding cleft and catalytic residues are conserved. ► Some of the conserved Ca2+ binding residues or secondary structures are altered. ► Novel direct interactions between Bsp165PelA and TGA form without Ca2+ participation.
Related Topics
Life Sciences Biochemistry, Genetics and Molecular Biology Biochemistry
Authors
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