7m6u
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of a circular permutation and computationally designed pro-enzyme of carboxypeptidase G2== | |
| + | <StructureSection load='7m6u' size='340' side='right'caption='[[7m6u]], [[Resolution|resolution]] 2.59Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[7m6u]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_sp._RS-16 Pseudomonas sp. RS-16] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7M6U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7M6U FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.59Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=7m6u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7m6u OCA], [https://pdbe.org/7m6u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7m6u RCSB], [https://www.ebi.ac.uk/pdbsum/7m6u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7m6u ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/CBPG_PSES6 CBPG_PSES6] Catalyzes the hydrolysis of reduced and non-reduced folates to pteroates and L-glutamate. This enzyme has a broad specificity. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | SignificanceProteins have shown promise as therapeutics and diagnostics, but their effectiveness is limited by our inability to spatially target their activity. To overcome this limitation, we developed a computationally guided method to design inactive proenzymes or zymogens, which are activated through cleavage by a protease. Since proteases are differentially expressed in various tissues and disease states, including cancer, these proenzymes could be targeted to the desired microenvironment. We tested our method on the therapeutically relevant protein carboxypeptidase G2 (CPG2). We designed Pro-CPG2s that are inhibited by 80 to 98% and are partially to fully reactivatable following protease treatment. The developed methodology, with further refinements, could pave the way for routinely designing protease-activated protein-based therapeutics and diagnostics that act in a spatially controlled manner. | ||
| - | + | Massively parallel, computationally guided design of a proenzyme.,Yachnin BJ, Azouz LR, White RE 3rd, Minetti CASA, Remeta DP, Tan VM, Drake JM, Khare SD Proc Natl Acad Sci U S A. 2022 Apr 12;119(15):e2116097119. doi:, 10.1073/pnas.2116097119. Epub 2022 Apr 4. PMID:35377786<ref>PMID:35377786</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 7m6u" style="background-color:#fffaf0;"></div> |
| - | [[Category: Yachnin | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Pseudomonas sp. RS-16]] | ||
| + | [[Category: Synthetic construct]] | ||
| + | [[Category: Khare SD]] | ||
| + | [[Category: Yachnin BJ]] | ||
Current revision
Crystal structure of a circular permutation and computationally designed pro-enzyme of carboxypeptidase G2
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