4niv: Difference between revisions
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== | ==Crystal structure of trypsiligase (K60E/N143H/Y151H/D189K trypsin) trigonal form== | ||
[[4niv]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NIV OCA]. | <StructureSection load='4niv' size='340' side='right' caption='[[4niv]], [[Resolution|resolution]] 1.00Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4niv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovin Bovin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NIV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NIV 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=GOL:GLYCEROL'>GOL</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4niw|4niw]], [[4nix|4nix]], [[4niy|4niy]]</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=4niv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4niv OCA], [http://pdbe.org/4niv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4niv RCSB], [http://www.ebi.ac.uk/pdbsum/4niv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4niv ProSAT]</span></td></tr> | |||
</table> | |||
<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> | |||
<ref | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4niv" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Trypsin|Trypsin]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bovin]] | |||
[[Category: Trypsin]] | [[Category: Trypsin]] | ||
[[Category: Parthier, C | [[Category: Parthier, C]] | ||
[[Category: Schoepfel, M | [[Category: Schoepfel, M]] | ||
[[Category: Stubbs, M T | [[Category: Stubbs, M T]] | ||
[[Category: Activation domain]] | [[Category: Activation domain]] | ||
[[Category: Enzyme design]] | [[Category: Enzyme design]] | ||
| Line 18: | Line 36: | ||
[[Category: Reverse proteolysis]] | [[Category: Reverse proteolysis]] | ||
[[Category: Serine proteinase]] | [[Category: Serine proteinase]] | ||
[[Category: Zymogen]] | [[Category: Zymogen]] | ||
Revision as of 15:47, 5 August 2016
Crystal structure of trypsiligase (K60E/N143H/Y151H/D189K trypsin) trigonal form
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