3HDF
Crystal structure of truncated endolysin R21 from phage 21
Summary for 3HDF
Entry DOI | 10.2210/pdb3hdf/pdb |
Related | 3HDE |
Descriptor | Lysozyme, NITRATE ION, GLYCEROL, ... (4 entities in total) |
Functional Keywords | lysozyme-like, antimicrobial, bacteriolytic enzyme, glycosidase, hydrolase, late protein |
Biological source | Enterobacteria phage P21 (Bacteriophage 21) |
Total number of polymer chains | 2 |
Total formula weight | 32648.92 |
Authors | Sun, Q.,Sacchettini, J.C. (deposition date: 2009-05-07, release date: 2009-11-03, Last modification date: 2024-10-16) |
Primary citation | Sun, Q.,Kuty, G.F.,Arockiasamy, A.,Xu, M.,Young, R.,Sacchettini, J.C. Regulation of a muralytic enzyme by dynamic membrane topology. Nat.Struct.Mol.Biol., 16:1192-1194, 2009 Cited by PubMed Abstract: R(21), the lysozyme of coliphage 21, has an N-terminal signal-anchor-release (SAR) domain that directs its secretion in a membrane-tethered, inactive form and then its release and activation in the periplasm. Both genetic and crystallographic studies show that the SAR domain, once extracted from the bilayer, refolds into the body of the enzyme and effects muralytic activation by repositioning one residue of the canonical lysozyme catalytic triad. PubMed: 19881499DOI: 10.1038/nsmb.1681 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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