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3HDE

Crystal structure of full-length endolysin R21 from phage 21

Summary for 3HDE
Entry DOI10.2210/pdb3hde/pdb
Related3HDF
DescriptorLysozyme (2 entities in total)
Functional Keywordslysozyme-like, antimicrobial, bacteriolytic enzyme, glycosidase, hydrolase, late protein
Biological sourceEnterobacteria phage P21 (Bacteriophage 21)
Total number of polymer chains4
Total formula weight72159.70
Authors
Sun, Q.,Arockiasamy, A.,McKee, E.,Caronna, E.,Sacchettini, J.C. (deposition date: 2009-05-07, release date: 2009-11-03, Last modification date: 2024-10-30)
Primary citationSun, 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: 19881499
DOI: 10.1038/nsmb.1681
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.95 Å)
Structure validation

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