4nix: Difference between revisions
New page: '''Unreleased structure''' The entry 4nix is ON HOLD Authors: Schoepfel, M., Parthier, C., Stubbs, M.T. Description: CRYSTAL STRUCTURE OF TRYPSILIGASE (K60E/N143H/Y151H/D189K TRYPSIN) ... |
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The | ==Crystal structure of trypsiligase (K60E/N143H/Y151H/D189K trypsin) orthorhombic form, zinc-bound== | ||
<StructureSection load='4nix' size='340' side='right'caption='[[4nix]], [[Resolution|resolution]] 1.30Å' 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]] 1.3Å</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. | |||
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> | |||
From MEDLINE®/PubMed®, 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]] | |||
Latest revision as of 09:44, 17 October 2024
Crystal structure of trypsiligase (K60E/N143H/Y151H/D189K trypsin) orthorhombic form, zinc-boundCrystal structure of trypsiligase (K60E/N143H/Y151H/D189K trypsin) orthorhombic form, zinc-bound
Structural highlights
FunctionPublication Abstract from PubMedAlthough 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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