Crystal structure of the antimicrobial peptidase lysostaphin from Staphylococcus simulans.
Bottom Line: The structure of the mature active enzyme confirms its expected organization into catalytic and cell-wall-targeting domains.It also indicates that the domains are mobile with respect to each other because of the presence of a highly flexible peptide linker.The high-resolution structures of the catalytic domain provide details of Zn(2+) coordination and may serve as a starting point for the engineering of lysostaphin variants with improved biotechnological characteristics. lysostaphin by x-ray crystallography (1, 2).
Affiliation: International Institute of Molecular and Cell Biology, Warsaw, Poland.Show MeSH
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Mentions: The lysostaphin catalytic domain shares key features of the M23 family peptidases 27. The core of these structures is an antiparallel β sheet that anchors the catalytic residues, which are grouped around a central Zn2+ cation (Fig. 5). Identification of this metal ion was confirmed crystallographically (by a drop in the anomalous density peak height at the metal ion sites passing from the absorption to the inflection point wavelength). In the high-resolution structures it is additionally supported by typical metal–ligand distances and similar temperature factors for the metal ion and the surrounding ligands. The Zn2+ ion is coordinated by His279 and Asp283 of the characteristic HxxxD motif and His362 of the HxH motif of LAS peptidases, as expected.
Affiliation: International Institute of Molecular and Cell Biology, Warsaw, Poland.