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| | <StructureSection load='4ke2' size='340' side='right'caption='[[4ke2]], [[Resolution|resolution]] 1.80Å' scene=''> | | <StructureSection load='4ke2' size='340' side='right'caption='[[4ke2]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4ke2]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseam Pseam]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KE2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4KE2 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4ke2]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudopleuronectes_americanus Pseudopleuronectes americanus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KE2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KE2 FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ke2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ke2 OCA], [http://pdbe.org/4ke2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ke2 RCSB], [http://www.ebi.ac.uk/pdbsum/4ke2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ke2 ProSAT]</span></td></tr> | + | </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=4ke2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ke2 OCA], [https://pdbe.org/4ke2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ke2 RCSB], [https://www.ebi.ac.uk/pdbsum/4ke2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ke2 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/ANPM_PSEAM ANPM_PSEAM] Contributes to protect fish blood from freezing at subzero sea water temperatures. Lowers the blood freezing point by about 1.1 degrees at a concentration of 0.1 mg/ml, and by about 1.5 degrees at a concentration of 0.2 mg/ml. Binds to nascent ice crystals and prevents further growth.<ref>PMID:15141201</ref> <ref>PMID:15716269</ref> <ref>PMID:18225917</ref> <ref>PMID:24531972</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Pseam]] | + | [[Category: Pseudopleuronectes americanus]] |
| - | [[Category: Allingham, J S]] | + | [[Category: Allingham JS]] |
| - | [[Category: Campbell, R L]] | + | [[Category: Campbell RL]] |
| - | [[Category: Davies, P L]] | + | [[Category: Davies PL]] |
| - | [[Category: Lin, F H]] | + | [[Category: Lin F-H]] |
| - | [[Category: Sun, T]] | + | [[Category: Sun T]] |
| - | [[Category: Antifreeze protein]]
| + | |
| - | [[Category: Dimeric alpha-helical bundle]]
| + | |
| Structural highlights
Function
ANPM_PSEAM Contributes to protect fish blood from freezing at subzero sea water temperatures. Lowers the blood freezing point by about 1.1 degrees at a concentration of 0.1 mg/ml, and by about 1.5 degrees at a concentration of 0.2 mg/ml. Binds to nascent ice crystals and prevents further growth.[1] [2] [3] [4]
Publication Abstract from PubMed
When polypeptide chains fold into a protein, hydrophobic groups are compacted in the center with exclusion of water. We report the crystal structure of an alanine-rich antifreeze protein that retains ~400 waters in its core. The putative ice-binding residues of this dimeric, four-helix bundle protein point inwards and coordinate the interior waters into two intersecting polypentagonal networks. The bundle makes minimal protein contacts between helices, but is stabilized by anchoring to the semi-clathrate water monolayers through backbone carbonyl groups in the protein interior. The ordered waters extend outwards to the protein surface and likely are involved in ice binding. This protein fold supports both the anchored-clathrate water mechanism of antifreeze protein adsorption to ice and the water-expulsion mechanism of protein folding.
An antifreeze protein folds with an interior network of more than 400 semi-clathrate waters.,Sun T, Lin FH, Campbell RL, Allingham JS, Davies PL Science. 2014 Feb 14;343(6172):795-8. doi: 10.1126/science.1247407. PMID:24531972[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Marshall CB, Fletcher GL, Davies PL. Hyperactive antifreeze protein in a fish. Nature. 2004 May 13;429(6988):153. doi: 10.1038/429153a. PMID:15141201 doi:http://dx.doi.org/10.1038/429153a
- ↑ Marshall CB, Chakrabartty A, Davies PL. Hyperactive antifreeze protein from winter flounder is a very long rod-like dimer of alpha-helices. J Biol Chem. 2005 May 6;280(18):17920-9. Epub 2005 Feb 16. PMID:15716269 doi:http://dx.doi.org/10.1074/jbc.M500622200
- ↑ Graham LA, Marshall CB, Lin FH, Campbell RL, Davies PL. Hyperactive antifreeze protein from fish contains multiple ice-binding sites. Biochemistry. 2008 Feb 19;47(7):2051-63. doi: 10.1021/bi7020316. Epub 2008 Jan, 29. PMID:18225917 doi:http://dx.doi.org/10.1021/bi7020316
- ↑ Sun T, Lin FH, Campbell RL, Allingham JS, Davies PL. An antifreeze protein folds with an interior network of more than 400 semi-clathrate waters. Science. 2014 Feb 14;343(6172):795-8. doi: 10.1126/science.1247407. PMID:24531972 doi:http://dx.doi.org/10.1126/science.1247407
- ↑ Sun T, Lin FH, Campbell RL, Allingham JS, Davies PL. An antifreeze protein folds with an interior network of more than 400 semi-clathrate waters. Science. 2014 Feb 14;343(6172):795-8. doi: 10.1126/science.1247407. PMID:24531972 doi:http://dx.doi.org/10.1126/science.1247407
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