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A model for interfacial activation in lipases from the structure of a fungal lipase-inhibitor complex
TLDR
It is proposed that the structure of the enzyme in this complex of R. miehei lipase with n-hexylphosphonate ethyl ester is equivalent to the activated state generated by the oil–water interface. Expand
Insights into trehalose synthesis provided by the structure of the retaining glucosyltransferase OtsA.
TLDR
The overall structure and the intimate details of the catalytic machinery reveal a striking similarity to glycogen phosphorylase, indicating a strong evolutionary link and suggesting a common catalytic mechanism. Expand
A serine protease triad forms the catalytic centre of a triacylglycerol lipase
TLDR
The X-ray structure of the Mucor miehei triglyceride lipase is reported and the atomic model obtained reveals a Ser .. His .. Asp trypsin-like catalytic triad with an active serine buried under a short helical fragment of a long surface loop. Expand
Crystal structure of GerE, the ultimate transcriptional regulator of spore formation in Bacillus subtilis.
TLDR
The crystal structure of GerE has been solved at 2.05 A resolution using multi-wavelength anomalous dispersion techniques and reveals the nature of the GerE dimer, which comprises four alpha-helices, of which the central pair forms a helix-turn-helix DNA-binding motif. Expand
The X6 "thermostabilizing" domains of xylanases are carbohydrate-binding modules: structure and biochemistry of the Clostridium thermocellum X6b domain.
TLDR
The data showed that X6b, but not X6a, increased the activity of the enzyme against insoluble xylan and bound specifically to xylooligosaccharides and various xylans, and it is proposed that this and related modules be re-assigned as family 22 carbohydrate-binding modules. Expand
Characterization and Three-dimensional Structures of Two Distinct Bacterial Xyloglucanases from Families GH5 and GH12*
TLDR
The enzymes, Paenibacillus pabuli XG5 and Bacillus licheniformis XG12, both display open active center grooves grafted upon their respective (β/α)8 and β-jelly roll folds, in which the side chain decorations of xyloglucan may be accommodated. Expand
Structural origins of the interfacial activation in Thermomyces (Humicola) lanuginosa lipase.
TLDR
Five new Thermomyces (formerly Humicola) lanuginosa lipase (TlL) crystal structures have been solved and compared with four previously reported structures of this enzyme, suggesting that the sequence of the structural changes, as exemplified in various TlL crystal structures, mirror those that may occur during interfacial activation. Expand
Structure and mechanism of a bacterial β-glucosaminidase having O-GlcNAcase activity
TLDR
Mutagenesis and kinetics studies show that the bacterial enzyme, very similarly to its human counterpart, operates via an unusual 'substrate-assisted' catalytic mechanism, which will inform the rational design of enzyme inhibitors. Expand
The Mechanisms by Which Family 10 Glycoside Hydrolases Bind Decorated Substrates*
TLDR
The crystal structure of the xylanase in complex with a range of decorated xylooligosaccharides reveals how this enzyme is able to hydrolyze substituted xylan and indicates that the complementarity in the binding of decorated substrates between the glycone and aglycone regions appears to be a conserved feature of GH10 xylanases. Expand
Crystal structures of fibronectin-binding sites from Staphylococcus aureus FnBPA in complex with fibronectin domains
TLDR
Four crystal structures of FnBPA and FnBPB, cell wall-attached proteins from S. aureus, have multiple, intrinsically disordered, high-affinity binding repeats (FnBRs) for Fn, revealing the roles of residues conserved and showing that there are few linker residues between FnBRs. Expand
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