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|
| Type |
Poster Presentation |
| Area |
Life Chemistry |
| Room No. |
Grand Ballroom |
| Time |
10월 19일 (금요일) 11:00~12:30 |
| Code |
LIFE.P-433 |
| Subject |
Structural insight into molecular mechanism of PsnB gained by homology modeling and molecular dynamics simulation |
| Authors |
JungUn Park, Seokhee Kim1,*, Chaok Seok1,*
Department of Chemistry, Seoul National University, Korea
1Division of Chemistry, Seoul National University, Korea
|
| Abstract |
Plesiocin is recently reported as a new kind of ribosomally-synthesized and post-translationally modified peptides (RiPPs). After a precursor peptide is synthesized by the ribosome, modifying enzyme binds to the leader peptide and builds ester bonds between the specific side chains of the core peptide. Since cyclic peptides are prone to have diverse biological activity, this macrocyclization reaction of PsnB has a possibility to be a versatile tool for biotechnology. In order to understand the molecular mechanism of PsnB, leader truncation experiments and core mutation study were attempted. However, detailed atomic interpretation is still unavailable. Therefore, structural insights were sought to be gained from homology modeling and molecular dynamics simulation. The Galaxy TBM program proposed several amino acid residues as key interacting residues and in vitro point mutation experiments are in progress simultaneously. Preliminary mutation study aligned fairly well with the model structure with minor differences to be revised in the model. In addition, molecular dynamics simulation was utilized to discuss the two hypotheses of coupling mechanism: one enzyme-driven folding or the fluctuation-driven folding. |
| E-mail |
eon93@snu.ac.kr |
|
122nd General Meeting of the KCS