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Two conformational states of Candida rugosa lipase
Comparison of this structure with the previously determined “open” form of this lipase, in which the active site is accessible to the solvent and presumably the substrate, shows that the transition between these 2 states requires only movement of the flap. Expand
Structure of a calpain Ca2+-binding domain reveals a novel EF-hand and Ca2+-induced conformational changes
A first view of the calcium-induced conformational changes is given, and consequently an insight into the mechanism of calcium induced activation in calpain is gained. Expand
High-resolution crystal structure of Arthrobacter aurescens chondroitin AC lyase: an enzyme-substrate complex defines the catalytic mechanism.
Comparison of this structure with that of chondroitinase AC from Flavobacterium heparinum (FlavoAC) provides an explanation for the exolytic and endolytic mode of action of ArthroAC and FlavoAC, respectively. Expand
Ser-His-Glu triad forms the catalytic site of the lipase from Geotrichum candidum
The three-dimensional structure of a lipase from G. candidum is reported at 2.2 Å resolution, and the catalytic triad of GCL is Ser-His-Glu, with glutamic acid replacing the usual aspartate. Expand
Structural and Functional Characterization of PseC, an Aminotransferase Involved in the Biosynthesis of Pseudaminic Acid, an Essential Flagellar Modification in Helicobacter pylori*
Helicobacter pylori flagellin is heavily glycosylated with the novel sialic acid-like nonulosonate, pseudaminic acid (Pse). The glycosylation process is essential for assembly of functional flagellarExpand
Crystal Structure of Heparinase II from Pedobacter heparinus and Its Complex with a Disaccharide Product*
The structure of the enzyme-product complex, combined with data from previously characterized mutations, allows us to propose a putative chemical mechanism of heparin and heparan-sulfate degradation. Expand
Crystal Structures of Escherichia coli ATP-Dependent Glucokinase and Its Complex with Glucose
The first structure determination of a microbial ATP-dependent glucokinase is reported, that from E. coli O157:H7, which is structurally similar to Saccharomyces cerevisiae hexokinase and human brain Hexokinase I but is distinct from the ADP-dependent GlKs. Expand
The structure of the RlmB 23S rRNA methyltransferase reveals a new methyltransferase fold with a unique knot.
The conserved residues in this novel family of 2'O-methyltransferases cluster in the knotted region, suggesting the location of the catalytic and AdoMet binding sites. Expand
Crystal structure of a dodecameric FMN‐dependent UbiX‐like decarboxylase (Pad1) from Escherichia coli O157: H7
The crystal structure of the flavoprotein Pad1 from Escherichia coli O157:H7 complexed with the cofactor FMN has been determined by the multiple anomalous diffraction method and refined at 2.0 Å resolution, forming a separate family, distinguishable from the HFCD family. Expand
The structure of the exopolyphosphatase (PPX) from Escherichia coli O157:H7 suggests a binding mode for long polyphosphate chains.
The crystal structure and analysis of the polyphosphate phosphatase PPX from Escherichia coli O157:H7 refined at 2.2 Angstroms resolution is reported, revealing close structural similarity between domains I and II of the two enzymes, with the PPX/GPPA representing an "open" state. Expand