Ontology highlight
ABSTRACT:
SUBMITTER: Sakamoto Y
PROVIDER: S-EPMC4460893 | biostudies-literature | 2015
REPOSITORIES: biostudies-literature
Sakamoto Yasumitsu Y Suzuki Yoshiyuki Y Iizuka Ippei I Tateoka Chika C Roppongi Saori S Fujimoto Mayu M Inaka Koji K Tanaka Hiroaki H Yamada Mitsugu M Ohta Kazunori K Gouda Hiroaki H Nonaka Takamasa T Ogasawara Wataru W Tanaka Nobutada N
Scientific reports 20150609
The dipeptidyl peptidase 11 from Porphyromonas gingivalis (PgDPP11) belongs to the S46 family of serine peptidases and preferentially cleaves substrates with Asp/Glu at the P1 position. The molecular mechanism underlying the substrate specificity of PgDPP11, however, is unknown. Here, we report the crystal structure of PgDPP11. The enzyme contains a catalytic domain with a typical double β-barrel fold and a recently identified regulatory α-helical domain. Crystal structure analyses, docking stud ...[more]