7a1h: Difference between revisions
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The | ==Crystal structure of wild-type CI2== | ||
<StructureSection load='7a1h' size='340' side='right'caption='[[7a1h]], [[Resolution|resolution]] 1.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7a1h]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Hordeum_vulgare Hordeum vulgare]. 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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</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='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> | |||
== 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> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 7a1h" style="background-color:#fffaf0;"></div> | ||
[[Category: Olsen | |||
[[Category: | ==See Also== | ||
[[Category: | *[[Chymotrypsin inhibitor 3D structures|Chymotrypsin inhibitor 3D structures]] | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Hordeum vulgare]] | |||
[[Category: Large Structures]] | |||
[[Category: Hamborg L]] | |||
[[Category: Olsen JG]] | |||
[[Category: Roche JV]] | |||
[[Category: Teilum K]] | |||
Latest revision as of 15:02, 1 February 2024
Crystal structure of wild-type CI2Crystal structure of wild-type CI2
Structural highlights
FunctionICI2_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. See AlsoReferences
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