7a1h: Difference between revisions
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==Crystal structure of wild-type CI2== | ==Crystal structure of wild-type CI2== | ||
<StructureSection load='7a1h' size='340' side='right'caption='[[7a1h]]' scene=''> | <StructureSection load='7a1h' size='340' side='right'caption='[[7a1h]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7A1H OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[7a1h]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Barley Barley]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7A1H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7A1H FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2ci2|2ci2]]</div></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=7a1h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7a1h OCA], [https://pdbe.org/7a1h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7a1h RCSB], [https://www.ebi.ac.uk/pdbsum/7a1h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7a1h ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[[https://www.uniprot.org/uniprot/ICI2_HORVU ICI2_HORVU]] Inhibits both subtilisin and chymotrypsin. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Most single point mutations destabilize folded proteins. Mutations that stabilize a protein typically only have a small effect and multiple mutations are often needed to substantially increase the stability. Multiple point mutations may act synergistically on the stability, and it is often not straightforward to predict their combined effect from the individual contributions. Here, we have applied an efficient in-cell assay in E. coli to select variants of the barley chymotrypsin inhibitor 2 with increased stability. We find two variants that are more than 3.8 kJ mol(-1) more stable than the wild-type. In one case, the increased stability is the effect of the single substitution D55G. The other case is a double mutant, L49I/I57V, which is 5.1 kJ mol(-1) more stable than the sum of the effects of the individual mutations. In addition to demonstrating the strength of our selection system for finding stabilizing mutations, our work also demonstrate how subtle conformational effects may modulate stability. | |||
Synergistic stabilization of a double mutant in chymotrypsin inhibitor 2 from a library screen in E. coli.,Hamborg L, Granata D, Olsen JG, Roche JV, Pedersen LE, Nielsen AT, Lindorff-Larsen K, Teilum K Commun Biol. 2021 Aug 18;4(1):980. doi: 10.1038/s42003-021-02490-7. PMID:34408246<ref>PMID:34408246</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7a1h" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Barley]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Hamborg L]] | [[Category: Hamborg, L]] | ||
[[Category: Olsen | [[Category: Olsen, J G]] | ||
[[Category: Roche | [[Category: Roche, J V]] | ||
[[Category: Teilum K]] | [[Category: Teilum, K]] | ||
[[Category: Protease inhibitor]] | |||
[[Category: Protein binding]] | |||
Revision as of 11:57, 29 September 2021
Crystal structure of wild-type CI2Crystal structure of wild-type CI2
Structural highlights
Function[ICI2_HORVU] Inhibits both subtilisin and chymotrypsin. Publication Abstract from PubMedMost single point mutations destabilize folded proteins. Mutations that stabilize a protein typically only have a small effect and multiple mutations are often needed to substantially increase the stability. Multiple point mutations may act synergistically on the stability, and it is often not straightforward to predict their combined effect from the individual contributions. Here, we have applied an efficient in-cell assay in E. coli to select variants of the barley chymotrypsin inhibitor 2 with increased stability. We find two variants that are more than 3.8 kJ mol(-1) more stable than the wild-type. In one case, the increased stability is the effect of the single substitution D55G. The other case is a double mutant, L49I/I57V, which is 5.1 kJ mol(-1) more stable than the sum of the effects of the individual mutations. In addition to demonstrating the strength of our selection system for finding stabilizing mutations, our work also demonstrate how subtle conformational effects may modulate stability. Synergistic stabilization of a double mutant in chymotrypsin inhibitor 2 from a library screen in E. coli.,Hamborg L, Granata D, Olsen JG, Roche JV, Pedersen LE, Nielsen AT, Lindorff-Larsen K, Teilum K Commun Biol. 2021 Aug 18;4(1):980. doi: 10.1038/s42003-021-02490-7. PMID:34408246[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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