7ddb: Difference between revisions
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==Crystal structure of fungal antifreeze protein with intermediate activity== | ==Crystal structure of fungal antifreeze protein with intermediate activity== | ||
<StructureSection load='7ddb' size='340' side='right'caption='[[7ddb]]' scene=''> | <StructureSection load='7ddb' size='340' side='right'caption='[[7ddb]], [[Resolution|resolution]] 1.72Å' 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=7DDB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7DDB FirstGlance]. <br> | <table><tr><td colspan='2'>[[7ddb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Typhula_ishikariensis Typhula ishikariensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7DDB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7DDB FirstGlance]. <br> | ||
</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=7ddb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ddb OCA], [https://pdbe.org/7ddb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ddb RCSB], [https://www.ebi.ac.uk/pdbsum/7ddb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ddb ProSAT]</span></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.72Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=7ddb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ddb OCA], [https://pdbe.org/7ddb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ddb RCSB], [https://www.ebi.ac.uk/pdbsum/7ddb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ddb ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q76CE7_TYPIS Q76CE7_TYPIS] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Antifreeze proteins (AFPs) inhibit ice growth by adsorbing onto specific ice planes. Microbial AFPs show diverse antifreeze activity and ice plane specificity, while sharing a common molecular scaffold. To probe the molecular mechanisms responsible for AFP activity, we here characterized the antifreeze activity and crystal structure of TisAFP7 from the snow mold fungus Typhula ishikariensis. TisAFP7 exhibited intermediate activity, with the ability to bind the basal plane, compared with a hyperactive isoform TisAFP8 and a moderately active isoform TisAFP6. Analysis of the TisAFP7 crystal structure revealed a bound-water network arranged in a zigzag pattern on the surface of the protein's ice-binding site (IBS). While the three AFP isoforms shared the water network pattern, the network on TisAFP7 IBS was not extensive, which was likely related to its intermediate activity. Analysis of the TisAFP7 crystal structure also revealed the presence of additional water molecules that form a ring-like network surrounding the hydrophobic side chain of a crucial IBS phenylalanine, which might be responsible for the increased adsorption of AFP molecule onto the basal plane. Based on these observations, we propose that the extended water network and hydrophobic hydration at IBS together determine the TisAFP activity. | |||
Characterization of microbial antifreeze protein with intermediate activity suggests that a bound-water network is essential for hyperactivity.,Khan NMU, Arai T, Tsuda S, Kondo H Sci Rep. 2021 Mar 16;11(1):5971. doi: 10.1038/s41598-021-85559-x. PMID:33727595<ref>PMID:33727595</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7ddb" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Antifreeze protein 3D structures|Antifreeze protein 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Typhula ishikariensis]] | |||
[[Category: Arai T]] | [[Category: Arai T]] | ||
[[Category: Khan NMMU]] | [[Category: Khan NMMU]] | ||
[[Category: Kondo H]] | [[Category: Kondo H]] | ||
[[Category: Tsuda S]] | [[Category: Tsuda S]] | ||
Latest revision as of 19:30, 29 November 2023
Crystal structure of fungal antifreeze protein with intermediate activityCrystal structure of fungal antifreeze protein with intermediate activity
Structural highlights
FunctionPublication Abstract from PubMedAntifreeze proteins (AFPs) inhibit ice growth by adsorbing onto specific ice planes. Microbial AFPs show diverse antifreeze activity and ice plane specificity, while sharing a common molecular scaffold. To probe the molecular mechanisms responsible for AFP activity, we here characterized the antifreeze activity and crystal structure of TisAFP7 from the snow mold fungus Typhula ishikariensis. TisAFP7 exhibited intermediate activity, with the ability to bind the basal plane, compared with a hyperactive isoform TisAFP8 and a moderately active isoform TisAFP6. Analysis of the TisAFP7 crystal structure revealed a bound-water network arranged in a zigzag pattern on the surface of the protein's ice-binding site (IBS). While the three AFP isoforms shared the water network pattern, the network on TisAFP7 IBS was not extensive, which was likely related to its intermediate activity. Analysis of the TisAFP7 crystal structure also revealed the presence of additional water molecules that form a ring-like network surrounding the hydrophobic side chain of a crucial IBS phenylalanine, which might be responsible for the increased adsorption of AFP molecule onto the basal plane. Based on these observations, we propose that the extended water network and hydrophobic hydration at IBS together determine the TisAFP activity. Characterization of microbial antifreeze protein with intermediate activity suggests that a bound-water network is essential for hyperactivity.,Khan NMU, Arai T, Tsuda S, Kondo H Sci Rep. 2021 Mar 16;11(1):5971. doi: 10.1038/s41598-021-85559-x. PMID:33727595[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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