Apo and acarbose-complex structures of the catalytic domain of GtfB from Streptococcus mutans and the truncated structure of the catalytic domain of GtfD are described.

Multiple catalytic domains in one chitinase have been shown to function synergistically during chitin degradation. Here, using biochemical and structural characterization, an insect chitinase was revealed to have two nonsynergistic catalytic domains, which may be involved in chitin synthesis instead of chitin degradation.

Three industrially relevant glucoamylase structures have been determined, revealing how the starch-binding module can adopt different orientations relative to the catalytic domain.

Crystallization of the tetramer of the head domain of influenza neuraminidase (NA) may result in a specific crystal with space group C222₁ and unit-cell parameters a ≃ 120, b ≃ 143, c ≃ 120 Å. The molecular packing of NA tetramers in this crystal intrinsically causes pathological imperfections, lattice-translocation defects, which complicate the structure determination.

The structure of human MICAL3 provides information about its mechanism.

Structures of the EAL domain of the E. coli direct oxygen sensor show the active site in a nonproductive conformation that has implications for the regulatory mechanism.

The 1.7 Å resolution crystal structure of peroxisomal multifunctional enzyme type 1 (MFE1) shows a conformation in which both catalytic sites are noncompetent. An analysis of the structures of its complexes with 3-ketodecanoyl-CoA suggests how conformational flexibility of MFE1 could be important for its function.

The identification, characterization and X-ray structure of a novel fungal GH24 muramidase from Trichophaea saccata is described in which an SH3-like cell-wall-binding domain was identified by structure comparisons in addition to its catalytic domain. A domain-walking approach was then used to identify a group of fungal muramidases that belong to a new GH family containing homologous SH3-like cell-wall-binding modules, and X-ray structures of the independent catalytic and SH3-like domains of three of them are reported.

Histone deacetylase 6 (HDAC6) is an emerging target for the treatment of various diseases such as cancer through selective inhibition. While the second catalytic domain (HDAC6 CD2) has been extensively studied, comparatively little research has focused on the first catalytic domain (HDAC6 CD1). This work provides new structural insights regarding inhibitor binding to HDAC6 CD1 enabled by the study of active-site mutants.

By determining the structure of the catalytic domain of the C. thermocellum cellulase CelT, the mechanism of function of the enzyme in the absence of an accessory module and the structural elements that might be responsible for its stability have been proposed.