Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

4LXC

The antimicrobial peptidase lysostaphin from Staphylococcus simulans

Summary for 4LXC
Entry DOI10.2210/pdb4lxc/pdb
Related1QWY 1R77 2B0P 2B13 2B44 3IT5 3IT7 4BH5 4QP5 4QPB
DescriptorLysostaphin, ZINC ION, SULFATE ION (3 entities in total)
Functional Keywordspeptidase family m23, peptidoglycan hydrolase, metallopeptidase, peptidoglycan, hydrolase
Biological sourceStaphylococcus simulans
Cellular locationSecreted: P10547
Total number of polymer chains4
Total formula weight113836.41
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: 2013-07-29, release date: 2014-07-09, Last modification date: 2023-09-20)
Primary citationSabala, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.5 Å)
Structure validation

235666

건을2025-05-07부터공개중

PDB statisticsPDBj update infoContact PDBjnumon