4QP5

Catalytic domain of the antimicrobial peptidase lysostaphin from Staphylococcus simulans crystallized in the presence of phosphate

Summary for 4QP5

• Entry DOI: 10.2210/pdb4qp5/pdb
• Related: 1QWY 1R77 2B0P 2B13 2B44 3IT5 3IT7 4BH5 4LXC 4QPB
• Descriptor: Lysostaphin, ZINC ION, PHOSPHATE ION, ... (5 entities in total)
• Functional Keywords: peptidase family m23, peptidoglycan amidase, metallopeptidase, peptidoglycan, hydrolase, extracellular
• Biological source: Staphylococcus simulans bv. staphylolyticus
• Cellular location: Secreted: P10547
• Total number of polymer chains: 2
• Total formula weight: 31181.30

Authors

Sabala, I.,Jagielska, E.,Bardelang, P.T.,Czapinska, H.,Dahms, S.O.,Sharpe, J.A.,James, R.,Than, M.E.,Thomas, N.R.,Bochtler, M. (deposition date: 2014-06-22, release date: 2014-07-16, Last modification date: 2023-09-20)

Primary citation

Sabala, I.,Jagielska, E.,Bardelang, P.T.,Czapinska, H.,Dahms, S.O.,Sharpe, J.A.,James, R.,Than, M.E.,Thomas, N.R.,Bochtler, M.
Crystal structure of the antimicrobial peptidase lysostaphin from Staphylococcus simulans.
Febs J., 281:4112-4122, 2014

PubMed Abstract: 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.

PubMed: 25039253
DOI: 10.1111/febs.12929

Experimental method

X-RAY DIFFRACTION (1.26 Å)