4nix: Difference between revisions

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-'''Unreleased structure'''
-The entry 4nix is ON HOLD
+==Crystal structure of trypsiligase (K60E/N143H/Y151H/D189K trypsin) orthorhombic form, zinc-bound==
+<StructureSection load='4nix' size='340' side='right'caption='[[4nix]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4nix]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NIX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NIX 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]] 1.3&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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=4nix FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nix OCA], [https://pdbe.org/4nix PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nix RCSB], [https://www.ebi.ac.uk/pdbsum/4nix PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nix ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/TRY1_BOVIN TRY1_BOVIN]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Although site-specific incorporation of artificial functionalities into proteins is an important tool in both basic and applied research, it can be a major challenge to protein chemists. Enzymatic protein modification is an attractive goal due to the inherent regio- and stereoselectivity of enzymes, yet their specificity remains a problem. As a result of the intrinsic reversibility of enzymatic reactions, proteinases can in principle catalyze ligation reactions. While this makes them attractive tools for site-specific protein bioconjugation, competing hydrolysis reactions limits their general use. Here we describe the design and application of a highly specific trypsin variant for the selective modification of N-terminal residues of diverse proteins with various reagents. The modification proceeds quantitatively under native (aqueous) conditions. We show that the variant has a disordered zymogen-like activation domain, effectively suppressing the hydrolysis reaction, which is converted to an active conformation in the presence of appropriate substrates.
-Authors: Schoepfel, M., Parthier, C., Stubbs, M.T.
+N-Terminal Protein Modification by Substrate-Activated Reverse Proteolysis.,Liebscher S, Schopfel M, Aumuller T, Sharkhuukhen A, Pech A, Hoss E, Parthier C, Jahreis G, Stubbs MT, Bordusa F Angew Chem Int Ed Engl. 2014 Feb 12. doi: 10.1002/anie.201307736. PMID:24520050<ref>PMID:24520050</ref>
-Description: CRYSTAL STRUCTURE OF TRYPSILIGASE (K60E/N143H/Y151H/D189K TRYPSIN) ORTHORHOMBIC FORM; ZINC-BOUND
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 4nix" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Trypsin 3D structures|Trypsin 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Bos taurus]]
+[[Category: Large Structures]]
+[[Category: Parthier C]]
+[[Category: Schoepfel M]]
+[[Category: Stubbs MT]]