3KL9

Crystal structure of PepA from Streptococcus pneumoniae

Summary for 3KL9

• Entry DOI: 10.2210/pdb3kl9/pdb
• Descriptor: Glutamyl aminopeptidase, ZINC ION (3 entities in total)
• Functional Keywords: glutamyl aminopeptidase, pepa, tetrahedral aminopeptidase, substrate specificity, metallopeptidase m42, aminopeptidase, hydrolase
• Biological source: Streptococcus pneumoniae
• Total number of polymer chains: 12
• Total formula weight: 459384.62

Authors

Kim, K.K.,Lee, S.,Kim, D. (deposition date: 2009-11-07, release date: 2010-02-02, Last modification date: 2023-11-01)

Primary citation

Kim, D.,San, B.H.,Moh, S.H.,Park, H.J.,Kim, D.Y.,Lee, S.,Kim, K.K.
Structural basis for the substrate specificity of PepA from Streptococcus pneumoniae, a dodecameric tetrahedral protease
Biochem.Biophys.Res.Commun., 391:431-436, 2010

PubMed 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.

PubMed: 19914209
DOI: 10.1016/j.bbrc.2009.11.075

Experimental method

X-RAY DIFFRACTION (2.7 Å)