8af1
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Beta-Lytic Protease from Lysobacter capsici== | |
| + | <StructureSection load='8af1' size='340' side='right'caption='[[8af1]], [[Resolution|resolution]] 1.57Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8af1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lysobacter_capsici Lysobacter capsici]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8AF1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8AF1 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]] 1.57Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=8af1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8af1 OCA], [https://pdbe.org/8af1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8af1 RCSB], [https://www.ebi.ac.uk/pdbsum/8af1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8af1 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The crystal structure of the Lysobacter capsici VKM B-2533(T) beta-lytic protease (Blp), a medicinally promising antimicrobial enzyme, was first solved. Blp was established to possess a folding characteristic of the M23 protease family. The groove of the Blp active site, as compared with that of the LasA structural homologue from Pseudomonas aeruginosa, was found to have amino acid differences. Biochemical analysis revealed no differences in the optimal reaction conditions for manifesting Blp and LasA bacteriolytic activities. At the same time, Blp had a broader range of action against living and autoclaved target cells. The results suggest that the distinction in the geometry of the active site and the charge of amino acid residues that form the active site groove can be important for the hydrolysis of different peptidoglycan types in target cells. | ||
| - | + | Structural and Functional Characterization of beta-lytic Protease from Lysobacter capsici VKM B-2533(T).,Afoshin A, Tishchenko S, Gabdulkhakov A, Kudryakova I, Galemina I, Zelenov D, Leontyevskaya E, Saharova S, Leontyevskaya Vasilyeva N Int J Mol Sci. 2022 Dec 17;23(24):16100. doi: 10.3390/ijms232416100. PMID:36555752<ref>PMID:36555752</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 8af1" style="background-color:#fffaf0;"></div> |
| - | [[Category: Afoshin | + | == References == |
| - | [[Category: | + | <references/> |
| - | [[Category: Tishchenko | + | __TOC__ |
| - | [[Category: | + | </StructureSection> |
| + | [[Category: Large Structures]] | ||
| + | [[Category: Lysobacter capsici]] | ||
| + | [[Category: Afoshin AS]] | ||
| + | [[Category: Gabdulkhakov AG]] | ||
| + | [[Category: Kudryakova IV]] | ||
| + | [[Category: Tishchenko TV]] | ||
| + | [[Category: Vasilyeva NV]] | ||
Current revision
Beta-Lytic Protease from Lysobacter capsici
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