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| ==Bovine trypsin in complex with microviridin J at pH 8.5== | | ==Bovine trypsin in complex with microviridin J at pH 8.5== |
- | <StructureSection load='4kts' size='340' side='right' caption='[[4kts]], [[Resolution|resolution]] 1.30Å' scene=''> | + | <StructureSection load='4kts' size='340' side='right'caption='[[4kts]], [[Resolution|resolution]] 1.30Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[4kts]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Microcystis_aeruginosa_mrc Microcystis aeruginosa mrc]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KTS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4KTS FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4kts]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [https://en.wikipedia.org/wiki/Microcystis_aeruginosa_MRC Microcystis aeruginosa MRC]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KTS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KTS FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr> |
- | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene></td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4kts FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kts OCA], [https://pdbe.org/4kts PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kts RCSB], [https://www.ebi.ac.uk/pdbsum/4kts PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kts ProSAT]</span></td></tr> |
- | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3myw|3myw]], [[4ktu|4ktu]]</td></tr>
| + | |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mdnA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=507735 Microcystis aeruginosa MRC])</td></tr>
| + | |
- | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] </span></td></tr>
| + | |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4kts FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kts OCA], [http://pdbe.org/4kts PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4kts RCSB], [http://www.ebi.ac.uk/pdbsum/4kts PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4kts ProSAT]</span></td></tr> | + | |
| </table> | | </table> |
| + | == Function == |
| + | [https://www.uniprot.org/uniprot/TRY1_BOVIN TRY1_BOVIN] |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| ==See Also== | | ==See Also== |
- | *[[Trypsin|Trypsin]] | + | *[[Trypsin 3D structures|Trypsin 3D structures]] |
| == References == | | == References == |
| <references/> | | <references/> |
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| </StructureSection> | | </StructureSection> |
| [[Category: Bos taurus]] | | [[Category: Bos taurus]] |
- | [[Category: Microcystis aeruginosa mrc]] | + | [[Category: Large Structures]] |
- | [[Category: Trypsin]] | + | [[Category: Microcystis aeruginosa MRC]] |
- | [[Category: Dittmann, E]] | + | [[Category: Dittmann E]] |
- | [[Category: Groll, M]] | + | [[Category: Groll M]] |
- | [[Category: Hertweck, C]] | + | [[Category: Hertweck C]] |
- | [[Category: Quitterer, F]] | + | [[Category: Quitterer F]] |
- | [[Category: Hydrolase]]
| + | |
- | [[Category: Hydrolase-hydrolase inhibitor complex]]
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- | [[Category: Natural product inhibitor]]
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- | [[Category: Protease]]
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- | [[Category: Serine protease]]
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| Structural highlights
Function
TRY1_BOVIN
Publication Abstract from PubMed
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.
Harnessing the evolvability of tricyclic microviridins to dissect protease-inhibitor interactions.,Weiz AR, Ishida K, Quitterer F, Meyer S, Kehr JC, Muller KM, Groll M, Hertweck C, Dittmann E Angew Chem Int Ed Engl. 2014 Apr 1;53(14):3735-8. doi: 10.1002/anie.201309721., Epub 2014 Mar 3. PMID:24591244[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Weiz AR, Ishida K, Quitterer F, Meyer S, Kehr JC, Muller KM, Groll M, Hertweck C, Dittmann E. Harnessing the evolvability of tricyclic microviridins to dissect protease-inhibitor interactions. Angew Chem Int Ed Engl. 2014 Apr 1;53(14):3735-8. doi: 10.1002/anie.201309721., Epub 2014 Mar 3. PMID:24591244 doi:http://dx.doi.org/10.1002/anie.201309721
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