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{{STRUCTURE_4niy|  PDB=4niy  |  SCENE=  }}
==Crystal structure of trypsiligase (K60E/N143H/Y151H/D189K trypsin) complexed to YRH-ecotin (M84Y/M85R/A86H ecotin)==
===Crystal structure of trypsiligase (K60E/N143H/Y151H/D189K trypsin) complexed to YRH-ecotin (M84Y/M85R/A86H ecotin)===
<StructureSection load='4niy' size='340' side='right' caption='[[4niy]], [[Resolution|resolution]] 2.84&Aring;' scene=''>
{{ABSTRACT_PUBMED_24520050}}
== Structural highlights ==
<table><tr><td colspan='2'>[[4niy]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovin Bovin] and [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NIY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NIY 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=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4niv|4niv]], [[4niw|4niw]], [[4nix|4nix]]</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">eco, eti, b2209, JW2197 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=4niy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4niy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4niy RCSB], [http://www.ebi.ac.uk/pdbsum/4niy PDBsum]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/ECOT_ECOLI ECOT_ECOLI]] General inhibitor of pancreatic serine proteases: inhibits chymotrypsin, trypsin, elastases, factor X, kallikrein as well as a variety of other proteases. The strength of inhibition does not appear to be correlated with a particular protease specificity.[HAMAP-Rule:MF_00706]
<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.


==Function==
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>
[[http://www.uniprot.org/uniprot/ECOT_ECOLI ECOT_ECOLI]] General inhibitor of pancreatic serine proteases: inhibits chymotrypsin, trypsin, elastases, factor X, kallikrein as well as a variety of other proteases. The strength of inhibition does not appear to be correlated with a particular protease specificity.[HAMAP-Rule:MF_00706]


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[4niy]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NIY OCA].
</div>


==See Also==
==See Also==
*[[Ecotin|Ecotin]]
*[[Ecotin|Ecotin]]
 
*[[Trypsin|Trypsin]]
==Reference==
== References ==
<ref group="xtra">PMID:024520050</ref><references group="xtra"/><references/>
<references/>
__TOC__
</StructureSection>
[[Category: Bovin]]
[[Category: Ecoli]]
[[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]]
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