4KTS
Bovine trypsin in complex with microviridin J at pH 8.5
Summary for 4KTS
| Entry DOI | 10.2210/pdb4kts/pdb |
| Related | 3MYW 4KTU |
| Related PRD ID | PRD_001086 |
| Descriptor | Cationic trypsin, Microviridin, CALCIUM ION, ... (5 entities in total) |
| Functional Keywords | serine protease, hydrolase, natural product inhibitor, protease, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor |
| Biological source | Microcystis aeruginosa MRC More |
| Cellular location | Secreted, extracellular space: P00760 |
| Total number of polymer chains | 2 |
| Total formula weight | 25195.35 |
| Authors | Quitterer, F.,Groll, M.,Hertweck, C.,Dittmann, E. (deposition date: 2013-05-21, release date: 2014-04-02, Last modification date: 2023-09-20) |
| Primary citation | Weiz, A.R.,Ishida, K.,Quitterer, F.,Meyer, S.,Kehr, J.C.,Muller, K.M.,Groll, M.,Hertweck, C.,Dittmann, E. Harnessing the evolvability of tricyclic microviridins to dissect protease-inhibitor interactions. Angew.Chem.Int.Ed.Engl., 53:3735-3738, 2014 Cited by PubMed Abstract: Understanding and controlling proteolysis is an important goal in therapeutic chemistry. Among the natural products specifically inhibiting proteases microviridins are particularly noteworthy. Microviridins are ribosomally produced and posttranslationally modified peptides that are processed into a unique, cagelike architecture. Here, we report a combined rational and random mutagenesis approach that provides fundamental insights into selectivity-conferring moieties of microviridins. The potent variant microviridin J was co-crystallized with trypsin, and for the first time the three-dimensional structure of microviridins was determined and the mode of inhibition revealed. PubMed: 24591244DOI: 10.1002/anie.201309721 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.3 Å) |
Structure validation
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