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]]

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

4nix is a 1 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.3Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TRY1_BOVIN

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Liebscher S, Schopfel M, Aumuller T, Sharkhuukhen A, Pech A, Hoss E, Parthier C, Jahreis G, Stubbs MT, Bordusa F. N-Terminal Protein Modification by Substrate-Activated Reverse Proteolysis. Angew Chem Int Ed Engl. 2014 Feb 12. doi: 10.1002/anie.201307736. PMID:24520050 doi:http://dx.doi.org/10.1002/anie.201307736

4nix, resolution 1.30Å

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