Journal: Biochemistry / Year: 2013 Title: Structure of signal peptide peptidase A with C-termini bound in the active sites: insights into specificity, self-processing, and regulation. Authors: Nam, S.E. / Paetzel, M.
A: Signal peptide peptidase SppA B: Signal peptide peptidase SppA C: Signal peptide peptidase SppA D: Signal peptide peptidase SppA E: Signal peptide peptidase SppA F: Signal peptide peptidase SppA G: Signal peptide peptidase SppA H: Signal peptide peptidase SppA
Mass: 18.015 Da / Num. of mol.: 221 / Source method: isolated from a natural source / Formula: H2O
Sequence details
LIMITED PROTEOLYSIS WAS CARRIED OUT ON SPPA_BS DELTA 1-25 K199A USING THERMOLYSIN, FOLLOWED BY SIZE- ...LIMITED PROTEOLYSIS WAS CARRIED OUT ON SPPA_BS DELTA 1-25 K199A USING THERMOLYSIN, FOLLOWED BY SIZE-EXCLUSION CHROMATOGRAPHY. THE CRYSTALLIZED AND SOLVED STRUCTURE IS A PROTEASE RESISTANT FRAGMENT OF SPPA_BS DELTA 1-25 K199A. USING N-TERMINAL SEQUENCING AND POSITIVE ELECTROSPRAY IONIZATION MASS SPECTROMETRY, THE PROTEASE RESISTANT FRAGMENT WAS IDENTIFIED AS SPPA_BS 51-295. THE REFINED OCTAMERIC STRUCTURE REVEALED THE CORE DOMAIN OF SPPA_BS 51-295, WITH THE C-TERMINI OF SPPA_BS BOUND IN THE EIGHT ACTIVE SITES. THE IDENTITY OF THE PEPTIDE WAS CONFIRMED AS 308-335 OF SPPA_BS(FKSEIDFLNMREILSQSGSPRMMYLYAK) BY TANDEM MASS SPECTROMETRY FRAGMENTATION ANALYSIS. CLEAR ELECTRON DESITY IS OBSERVED FOR 326-335 (SPRMMYLYAK). WHAT HAS BEEN CRYSTALLIZED IS SPPA_BS RESIDUES: 51-295 & 308-335
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Experimental details
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Experiment
Experiment
Method: X-RAY DIFFRACTION / Number of used crystals: 1
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Sample preparation
Crystal
Density Matthews: 2.48 Å3/Da / Density % sol: 50.42 %
Crystal grow
Temperature: 298.15 K / Method: vapor diffusion, sitting drop / pH: 8.5 Details: 100mM TRIS, 23% TERT-BUTANOL UNDER PARAFFIN OIL, VAPOR DIFFUSION, SITTING DROP, temperature 298.15K, pH 8.5
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