View source for 2jet


==Crystal structure of a trypsin-like mutant (S189D , A226G) chymotrypsin.==
<StructureSection load='2jet' size='340' side='right'caption='[[2jet]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2jet]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JET OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JET 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]] 2.2&#8491;</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=2jet FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jet OCA], [https://pdbe.org/2jet PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jet RCSB], [https://www.ebi.ac.uk/pdbsum/2jet PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jet ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CTRB1_RAT CTRB1_RAT] 
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/je/2jet_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2jet ConSurf].
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== Publication Abstract from PubMed ==
The crystal structure of the S189D+A226G rat chymotrypsin-B mutant has been determined at 2.2 A resolution. This mutant is the most trypsin-like mutant so far in the line of chymotrypsin-to-trypsin conversions, aiming for a more complete understanding of the structural basis of substrate specificity in pancreatic serine proteases. A226G caused significant rearrangements relative to S189D chymotrypsin, allowing an internal conformation of Asp189 which is close to that in trypsin. Serious distortions remain, however, in the activation domain, including zymogen-like features. The pH-profile of activity suggests that the conformation of the S1-site of the mutant is influenced also by the P1 residue of the substrate.

The Crystal Structure of a Trypsin-like Mutant Chymotrypsin: The Role of Position 226 in the Activity and Specificity of S189D Chymotrypsin.,Jelinek B, Katona G, Fodor K, Venekei I, Graf L Protein J. 2007 Sep 6;. PMID:17805946<ref>PMID:17805946</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 2jet" style="background-color:#fffaf0;"></div>

==See Also==
*[[Chymotrypsin 3D structures|Chymotrypsin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Fodor K]]
[[Category: Graf L]]
[[Category: Jelinek B]]
[[Category: Katona G]]
[[Category: Venekei I]]