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UnknownX-ray crystallographic structure of the Norwalk virus protease at 1.5-A resolution.
Norwalk virus (NV), a member of the Caliciviridae family, is the major cause of acute, epidemic, viral gastroenteritis. The NV genome is a positive sense, single-stranded RNA that encodes three open reading frames (ORFs). The first ORF produces a polyprotein that is processed by the viral cysteine p...
S-EPMC1472067 | biostudies-literature
UnknownMapping the determinants of catalysis and substrate specificity of the antibiotic resistance enzyme CTX-M β-lactamase.
CTX-M β-lactamases are prevalent antibiotic resistance enzymes and are notable for their ability to rapidly hydrolyze the extended-spectrum cephalosporin, cefotaxime. We hypothesized that the active site sequence requirements of CTX-M-mediated hydrolysis differ between classes of β-lactam antibiotic...
S-EPMC9837174 | biostudies-literature
UnknownCarbohydrate-Binding Module and Linker Allow Cold Adaptation and Salt Tolerance of Maltopentaose-Forming Amylase From Marine Bacterium Saccharophagus degradans 2-40 T.
Marine extremophiles produce cold-adapted and/or salt-tolerant enzymes to survive in harsh conditions. These enzymes are naturally evolved with unique structural features that confer a high level of flexibility, solubility and substrate-binding ability compared to mesophilic and thermostable homolog...
S-EPMC8317173 | biostudies-literature
UnknownBroadly cross-reactive human antibodies that inhibit genogroup I and II noroviruses.
The rational development of norovirus vaccine candidates requires a deep understanding of the antigenic diversity and mechanisms of neutralization of the virus. Here, we isolate and characterize a panel of broadly cross-reactive naturally occurring human monoclonal IgMs, IgAs and IgGs reactive with ...
S-EPMC8280134 | biostudies-literature
UnknownStructural basis of glycan interaction in gastroenteric viral pathogens.
A critical event in the life cycle of a virus is its initial attachment to host cells. This involves recognition by the viruses of specific receptors on the cell surface, including glycans. Viruses typically exhibit strain-dependent variations in recognizing specific glycan receptors, a feature that...
S-EPMC4251800 | biostudies-literature
UnknownStructural basis of glycan specificity in neonate-specific bovine-human reassortant rotavirus.
Strain-dependent variation of glycan recognition during initial cell attachment of viruses is a critical determinant of host specificity, tissue-tropism and zoonosis. Rotaviruses (RVs), which cause life-threatening gastroenteritis in infants and children, display significant genotype-dependent varia...
S-EPMC4589887 | biostudies-literature
UnknownGII.4 Norovirus Protease Shows pH-Sensitive Proteolysis with a Unique Arg-His Pairing in the Catalytic Site.
Human noroviruses (NoVs) are the main cause of epidemic and sporadic gastroenteritis. Phylogenetically, noroviruses are divided into seven genogroups, with each divided into multiple genotypes. NoVs belonging to genogroup II and genotype 4 (GII.4) are globally most prevalent. Genetic diversity among...
S-EPMC6401421 | biostudies-literature
UnknownStructure of orthoreovirus RNA chaperone σNS, a component of viral replication factories.
The mammalian orthoreovirus (reovirus) σNS protein is required for formation of replication compartments that support viral genome replication and capsid assembly. Despite its functional importance, a mechanistic understanding of σNS is lacking. We conducted structural and biochemical analyses of a ...
S-EPMC10950856 | biostudies-literature
UnknownMRC2020: improvements to Ximdisp and the MRC image-processing programs.
The great success of single-particle electron cryo-microscopy (cryoEM) during the last decade has involved the development of powerful new computer programs and packages that guide the user along a recommended processing workflow, in which the wisdom and choices made by the developers help everyone,...
S-EPMC10478516 | biostudies-literature
UnknownStructural basis of the stereoselective formation of the spirooxindole ring in the biosynthesis of citrinadins.
Prenylated indole alkaloids featuring spirooxindole rings possess a 3R or 3S carbon stereocenter, which determines the bioactivities of these compounds. Despite the stereoselective advantages of spirooxindole biosynthesis compared with those of organic synthesis, the biocatalytic mechanism for contr...
S-EPMC8260726 | biostudies-literature
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