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Results describe genetics and biochemical aspects of Staphylococcus aureus DNA ligase in terms of cloning, expression, and N- and C- terminal domain sequencing. Data suggest that conservation of key functional domains in the enzyme makes it an important broad-spectrum antibacterial target that can be exploited in the screening of antibiotics.

It has been possible to identify the stereocentres of the pacidamycins. All proteinogenic amino acids are of the natural, (S) configuration, with the DABA residue being of the (2S,3S) configuration.

The existence of a temperature-sensitive lethal mutant gene in the cell membrane of Staphylococcus aureus may trigger genetic variations in the pathogenic bacteria. This gene particularly affects the strain's two-component histidine kinase-response regulator gene. Laboratory results further revealed the lethal mutant's hypersusceptibility to lincosamide antibiotics and macrolide even in pervasive levels of ermB resistance determinant. DNA analysis further highlighted the two-component system's ability to regulate cell wall or membrane composition.

X-ray diffraction techniques determine the three-dimensional structure and architecture of FKBP13. FKBP13 is made up of a four-stranded beta sheet surrounded by a short seven-residue alpha helix. The protein structure of FKBP13 causes poor calcineurinization.

The specificity of the interaction between the FKBP12-FK506 complex and the protein phosphatase calcineurin (CN) gained through the construction of FKBP12-FKBP13 chimeric proteins is studied. Results reveal that among the known FKBPs, only FKBP12 is capable of binding with high affinity to CN and mediate the actins of FK506 in T cells. It is also found that specific mutations can alter the potential biological actions of these immunophilins.

Examines the atomic structure of the immunophiln FKBP13-FK506 complex with emphasis on the composite binding surface for calcineurin.