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3ROH

Crystal Structure of Leukotoxin (LukE) from Staphylococcus aureus subsp. aureus COL.

Summary for 3ROH
Entry DOI10.2210/pdb3roh/pdb
DescriptorLeucotoxin LukEv, TRIETHYLENE GLYCOL, CHLORIDE ION, ... (4 entities in total)
Functional Keywordsstructural genomics, center for structural genomics of infectious diseases, csgid, leukocidin-like, leukocidin, pore-forming toxin, membrane and cell surface proteins and peptides, toxin
Biological sourceStaphylococcus aureus subsp. aureus NCTC 8325
Cellular locationSecreted : Q2FXB0
Total number of polymer chains1
Total formula weight37259.57
Authors
Primary citationNocadello, S.,Minasov, G.,Shuvalova, L.,Dubrovska, I.,Sabini, E.,Bagnoli, F.,Grandi, G.,Anderson, W.F.
Crystal structures of the components of the Staphylococcus aureus leukotoxin ED.
Acta Crystallogr.,Sect.D, 72:113-120, 2016
Cited by
PubMed Abstract: Staphylococcal leukotoxins are a family of β-barrel, bicomponent, pore-forming toxins with membrane-damaging functions. These bacterial exotoxins share sequence and structural homology and target several host-cell types. Leukotoxin ED (LukED) is one of these bicomponent pore-forming toxins that Staphylococcus aureus produces in order to suppress the ability of the host to contain the infection. The recent delineation of the important role that LukED plays in S. aureus pathogenesis and the identification of its protein receptors, combined with its presence in S. aureus methicillin-resistant epidemic strains, establish this leukocidin as a possible target for the development of novel therapeutics. Here, the crystal structures of the water-soluble LukE and LukD components of LukED have been determined. The two structures illustrate the tertiary-structural variability with respect to the other leukotoxins while retaining the conservation of the residues involved in the interaction of the protomers in the bipartite leukotoxin in the pore complex.
PubMed: 26894539
DOI: 10.1107/S2059798315023207
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.2 Å)
Structure validation

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数据于2024-11-06公开中

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