Structure-Function Relationship of Aminopeptidase P from Pseudomonas aeruginosa.
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ABSTRACT:
SUBMITTER: Peng CT
PROVIDER: S-EPMC5723419 | biostudies-literature | 2017
REPOSITORIES: biostudies-literature
Publications
Structure-Function Relationship of Aminopeptidase P from <i>Pseudomonas aeruginosa</i>.
Peng Cui-Ting CT Liu Li L Li Chang-Cheng CC He Li-Hui LH Li Tao T Shen Ya-Lin YL Gao Chao C Wang Ning-Yu NY Xia Yong Y Zhu Yi-Bo YB Song Ying-Jie YJ Lei Qian Q Yu Luo-Ting LT Bao Rui R
Frontiers in microbiology 20171205
<i>PepP</i> is a virulence-associated gene in <i>Pseudomonas aeruginosa</i>, making it an attractive target for anti<i>-P. aeruginosa</i> drug development. The encoded protein, aminopeptidases P (Pa-PepP), is a type of X-prolyl peptidase that possesses diverse biological functions. The crystal structure verified its canonical pita-bread fold and functional tetrameric assembly, and the functional studies measured the influences of different metal ions on the activity. A trimetal manganese cluster ...[more]
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