1i3b: Difference between revisions
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[[ | ==THEORETICAL BETA-HELIX MODEL OF A PLANT ANTIFREEZE PROTEIN FROM LOLIUM PERENNE.== | ||
<StructureSection load='1i3b' size='340' side='right'caption='[[1i3b]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I3B 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=1i3b FirstGlance], [https://www.ebi.ac.uk/pdbsum/1i3b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i3b ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Antifreeze proteins (AFPs), found in certain organisms enduring freezing environments, have the ability to inhibit damaging ice crystal growth. Recently, the repetitive primary sequence of the AFP of perennial ryegrass, Lolium perenne, was reported. This macromolecular antifreeze has high ice recrystallization inhibition activity but relatively low thermal hysteresis activity. We present here a theoretical three-dimensional model of this 118-residue plant protein based on a beta-roll domain with eight loops of 14-15 amino acids. The fold is supported by a conserved valine hydrophobic core and internal asparagine ladders at either end of the roll. Our model, which is the first proposed for a plant AFP, displays two putative, opposite-facing, ice-binding sites with surface complementarity to the prism face of ice. The juxtaposition of the two imperfect ice-binding surfaces suggests an explanation for the protein's inferior thermal hysteresis but superior ice recrystallization inhibition activity and activity when compared with fish and insect AFPs. | |||
A theoretical model of a plant antifreeze protein from Lolium perenne.,Kuiper MJ, Davies PL, Walker VK Biophys J. 2001 Dec;81(6):3560-5. PMID:11721016<ref>PMID:11721016</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
<div class="pdbe-citations 1i3b" style="background-color:#fffaf0;"></div> | |||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Theoretical Model]] | |||
[[Category: Large Structures]] | |||
[[Category: Davies, P L]] | [[Category: Davies, P L]] | ||
[[Category: Kuiper, M J]] | [[Category: Kuiper, M J]] | ||
[[Category: Walker, V K]] | [[Category: Walker, V K]] | ||
Latest revision as of 13:56, 4 August 2021
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THEORETICAL BETA-HELIX MODEL OF A PLANT ANTIFREEZE PROTEIN FROM LOLIUM PERENNE.THEORETICAL BETA-HELIX MODEL OF A PLANT ANTIFREEZE PROTEIN FROM LOLIUM PERENNE.
Structural highlights
Publication Abstract from PubMedAntifreeze proteins (AFPs), found in certain organisms enduring freezing environments, have the ability to inhibit damaging ice crystal growth. Recently, the repetitive primary sequence of the AFP of perennial ryegrass, Lolium perenne, was reported. This macromolecular antifreeze has high ice recrystallization inhibition activity but relatively low thermal hysteresis activity. We present here a theoretical three-dimensional model of this 118-residue plant protein based on a beta-roll domain with eight loops of 14-15 amino acids. The fold is supported by a conserved valine hydrophobic core and internal asparagine ladders at either end of the roll. Our model, which is the first proposed for a plant AFP, displays two putative, opposite-facing, ice-binding sites with surface complementarity to the prism face of ice. The juxtaposition of the two imperfect ice-binding surfaces suggests an explanation for the protein's inferior thermal hysteresis but superior ice recrystallization inhibition activity and activity when compared with fish and insect AFPs. A theoretical model of a plant antifreeze protein from Lolium perenne.,Kuiper MJ, Davies PL, Walker VK Biophys J. 2001 Dec;81(6):3560-5. PMID:11721016[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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