4d8e

High resolution structures of monomeric S. pyogenes SpeB reveals role of glycine-rich active site loop

spinqualitylabelsall models 4d8e, resolution 1.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4d8e is a 1 chain structure with sequence from Streptococcus pyogenes ATCC 10782. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.497Å Ligands: E64, NO3 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Cysteine protease SpeB is secreted from Streptococcus pyogenes and has been studied as a potential virulence factor since its identification almost 70 years ago. Here, we report the crystal structures of apo mature SpeB to 1.06 Angstrom resolution as well as complexes with the general cysteine protease inhibitor E64 and a novel substrate mimetic peptide inhibitor. These structures uncover conformational changes associated with maturation of SpeB from the inactive zymogen to its active form and identify the residues required for substrate binding. With the use of a newly developed fluorogenic tri-peptide substrate to measure SpeB activity, we determined IC50 values for E64 and our new peptide inhibitor and the effects of mutations within the C-terminal, active-site loop. The structures and mutational analysis suggest conformational movements of the glycine-rich C-terminal loop are important for the recognition and recruitment of biological substrates and release of hydrolyzed products. Ultra-high and high resolution structures and mutational analysis of monomeric Streptococcus pyogenes SpeB reveal a functional role for the glycine-rich C-terminal loop.,Gonzalez-Paez GE, Wolan DW J Biol Chem. 2012 May 29. PMID:22645124 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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