4nix: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Crystal structure of trypsiligase (K60E/N143H/Y151H/D189K trypsin) orthorhombic form, zinc-bound== | ==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=''> | <StructureSection load='4nix' size='340' side='right'caption='[[4nix]], [[Resolution|resolution]] 1.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4nix]] 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=4NIX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NIX FirstGlance]. <br> | <table><tr><td colspan='2'>[[4nix]] 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=4NIX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NIX FirstGlance]. <br> | ||
| Line 26: | Line 26: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Bovin]] | [[Category: Bovin]] | ||
[[Category: Large Structures]] | |||
[[Category: Trypsin]] | [[Category: Trypsin]] | ||
[[Category: Parthier, C]] | [[Category: Parthier, C]] | ||
Revision as of 11:28, 10 April 2019
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
Publication 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
|
| ||||||||||||||||||||