Johan P. Turkenburg

TL;DR: The structure is related to those of known β‐hydroxyacid dehydrogenases, except that the essential lysine, which serves as an acid/base in the (de)protonation of the nascent alcohol in those enzymes, is replaced by an aspartate residue, Asp187 in Q1EQE0.

TL;DR: The work reveals a paradigm for formation of fibrils on the 100-nm scale and suggests that biofilm accumulation occurs through a mechanism distinct from the “zinc zipper.”

TL;DR: By introducing a single mutation without direct ligand contacts, a >1000-fold change in sialic acid binding affinity is observed in the Haemophilus influenzae virulence protein SiaP, suggesting that solvent structure is an evolutionary con-straint on protein sequence that contributes to ligand affinity and selectivity.

TL;DR: The 3-D structure of BaPul13A, a pullulanase from the bacterium Bacillus acidopullulyticus, was solved by single isomorphous replacement using an ‘‘in-house’’ uranyl derivative and subsequently refined in two different crystal forms.

TL;DR: It is demonstrated that HylP1, a phage tail-fiber protein responsible for the digestion of the S. pyogenes hyaluronan capsule during phage infection, is ahyaluronate lyase, and 3D structure reveals an unusual triple-stranded beta-helical structure and provides insight into the structural basis forphage tail assembly and the role of phage Tail proteins in virulence.