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Crystal structure of the antimicrobial peptidase lysostaphin from Staphylococcus simulans
Author(s) -
Sabala Izabela,
Jagielska Elzbieta,
Bardelang Philip T.,
Czapinska Honorata,
Dahms Sven O.,
Sharpe Jason A.,
James Richard,
Than Manuel E.,
Thomas Neil R.,
Bochtler Matthias
Publication year - 2014
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.12929
Subject(s) - lysostaphin , bacteriocin , staphylococcus aureus , biology , enzyme , chemistry , microbiology and biotechnology , bacteria , antimicrobial , genetics , biochemistry
Staphylococcus simulans biovar staphylolyticus lysostaphin efficiently cleaves Staphylococcus aureus cell walls. The protein is in late clinical trials as a topical anti‐staphylococcal agent, and can be used to prevent staphylococcal growth on artificial surfaces. Moreover, the gene has been both stably engineered into and virally delivered to mice or livestock to obtain resistance against staphylococci. Here, we report the first crystal structure of mature lysostaphin and two structures of its isolated catalytic domain at 3.5, 1.78 and 1.26 Å resolution, respectively. 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. Structured digital abstractlysostaphin by x-ray crystallography ( 1 , 2 ).