3owv

Structural insights into catalytic and substrate binding mechanisms of the strategic EndA nuclease from Streptococcus pneumoniae

spinqualitylabelsall models 3owv, resolution 1.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3owv is a 2 chain structure with sequence from Streptococcus pneumoniae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CL, MG Related: 1g8t, 1zm8, 3ism, 1oup Gene: endA, SP_1964 (Streptococcus pneumoniae) Resources: FirstGlance, OCA, RCSB, PDBsum Function [NUCE_STRPN] By degrading DNA that enters the cell, plays a role in the competence of cells to be transformed. Publication Abstract from PubMed EndA is a sequence non-specific endonuclease that serves as a virulence factor during Streptococcus pneumoniae infection. Expression of EndA provides a strategy for evasion of the host's neutrophil extracellular traps, digesting the DNA scaffold structure and allowing further invasion by S. pneumoniae. To define mechanisms of catalysis and substrate binding, we solved the structure of EndA at 1.75 A resolution. The EndA structure reveals a DRGH (Asp-Arg-Gly-His) motif-containing betabetaalpha-metal finger catalytic core augmented by an interesting 'finger-loop' interruption of the active site alpha-helix. Subsequently, we delineated DNA binding versus catalytic functionality using structure-based alanine substitution mutagenesis. Three mutants, H154A, Q186A and Q192A, exhibited decreased nuclease activity that appears to be independent of substrate binding. Glu205 was found to be crucial for catalysis, while residues Arg127/Lys128 and Arg209/Lys210 contribute to substrate binding. The results presented here provide the molecular foundation for development of specific antibiotic inhibitors for EndA. Structural insights into catalytic and substrate binding mechanisms of the strategic EndA nuclease from Streptococcus pneumoniae.,Moon AF, Midon M, Meiss G, Pingoud A, London RE, Pedersen LC Nucleic Acids Res. 2010 Nov 26. PMID:21113026 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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