Structural basis for the substrate specificity of PepA from Streptococcus pneumoniae, a dodecameric tetrahedral protease |
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Authors: | Doyoun Kim Sang Hyun Moh Hyejin Park Sangho Lee Kyeong Kyu Kim |
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Institution: | a Department of Molecular and Cell Biology, Samsung Biomedical Research Institute, Sungkyunkwan University School of Medicine, Suwon 440-746, South Korea b Sungkyunkwan Advanced Institute of Nanotechnology, Sungkyunkwan University, Suwon 440-746, South Korea c Department of Biological Science, Sungkyunkwan University, Suwon 440-746, South Korea |
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Abstract: | Regulated cytosolic proteolysis is one of the key cellular processes ensuring proper functioning of a cell. M42 family proteases show a broad spectrum of substrate specificities, but the structural basis for such diversity of the substrate specificities is lagging behind biochemical data. Here we report the crystal structure of PepA from Streptococcus pneumoniae, a glutamyl aminopeptidase belonging to M42 family (SpPepA). We found that Arg-257 in the substrate binding pocket is strategically positioned so that Arg-257 can make electrostatic interactions with the acidic residue of a substrate at its N-terminus. Structural comparison of the substrate binding pocket of the M42 family proteases, along with the structure-based multiple sequence alignment, argues that the appropriate electrostatic interactions contribute to the selective substrate specificity of SpPepA. |
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Keywords: | PepA glutamyl aminopeptidase from Streptococcus pneumoniae S1 pocket substrate binding pocket 1 TRI tricorn protease PhTET1 PH0519 from P horikoshii PhTET2 PH1527 from P horikoshii PhTET3 PH1821 from P horikoshii |
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