2py2: Difference between revisions
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==Structure of Herring Type II Antifreeze Protein== | ==Structure of Herring Type II Antifreeze Protein== | ||
<StructureSection load='2py2' size='340' side='right' caption='[[2py2]], [[Resolution|resolution]] 1.70Å' scene=''> | <StructureSection load='2py2' size='340' side='right'caption='[[2py2]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2py2]] is a 6 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2py2]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Atlantic_herring Atlantic herring]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PY2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PY2 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></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hAFP ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hAFP ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7950 Atlantic herring])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2py2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2py2 OCA], [https://pdbe.org/2py2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2py2 RCSB], [https://www.ebi.ac.uk/pdbsum/2py2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2py2 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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==See Also== | ==See Also== | ||
*[[Antifreeze protein|Antifreeze protein]] | *[[Antifreeze protein 3D structures|Antifreeze protein 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Atlantic herring]] | [[Category: Atlantic herring]] | ||
[[Category: Large Structures]] | |||
[[Category: Hew, C L]] | [[Category: Hew, C L]] | ||
[[Category: Li, Z]] | [[Category: Li, Z]] | ||
Revision as of 18:35, 17 June 2021
Structure of Herring Type II Antifreeze ProteinStructure of Herring Type II Antifreeze Protein
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedIn order to survive under extremely cold environments, many organisms produce antifreeze proteins (AFPs). AFPs inhibit the growth of ice crystals and protect organisms from freezing damage. Fish AFPs can be classified into five distinct types based on their structures. Here we report the structure of herring AFP (hAFP), a Ca(2+)-dependent fish type II AFP. It exhibits a fold similar to the C-type (Ca(2+)-dependent) lectins with unique ice-binding features. The 1.7 A crystal structure of hAFP with bound Ca(2+) and site-directed mutagenesis reveal an ice-binding site consisting of Thr96, Thr98 and Ca(2+)-coordinating residues Asp94 and Glu99, which initiate hAFP adsorption onto the [10-10] prism plane of the ice lattice. The hAFP-ice interaction is further strengthened by the bound Ca(2+) through the coordination with a water molecule of the ice lattice. This Ca(2+)-coordinated ice-binding mechanism is distinct from previously proposed mechanisms for other AFPs. However, phylogenetic analysis suggests that all type II AFPs evolved from the common ancestor and developed different ice-binding modes. We clarify the evolutionary relationship of type II AFPs to sugar-binding lectins. Structure and evolutionary origin of Ca2+-dependent herring type II antifreeze protein.,Liu Y, Li Z, Lin Q, Kosinski J, Seetharaman J, Bujnicki JM, Sivaraman J, Hew CL PLoS ONE. 2007 Jun 20;2(6):e548. PMID:17579720[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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