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3ult

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Crystal structure of an ice-binding protein from the perennial ryegrass, Lolium perenne

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Retrieved from "http://52.214.119.220/wiki/index.php/3ult"

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 <StructureSection load='3ult' size='340' side='right'caption='[[3ult]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3ult]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Festuca_perennis Festuca perennis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ULT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ULT FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3ult]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lolium_perenne Lolium perenne]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ULT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ULT FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=EOH:ETHANOL'>EOH</scene></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]] 1.4&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">IRI3 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4522 Festuca perennis])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=EOH:ETHANOL'>EOH</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=3ult FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ult OCA], [https://pdbe.org/3ult PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ult RCSB], [https://www.ebi.ac.uk/pdbsum/3ult PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ult ProSAT]</span></td></tr>
 </table>
-<div style="background-color:#fffaf0;">
+== Function ==
-== Publication Abstract from PubMed ==
+[https://www.uniprot.org/uniprot/B5T007_LOLPR B5T007_LOLPR]
-The grass Lolium perenne produces an ice-binding protein (LpIBP) that helps this perennial tolerate freezing by inhibiting the recrystallization of ice. Ice-binding proteins (IBPs) are also produced by freeze-avoiding organisms to halt the growth of ice and are better known as antifreeze proteins (AFPs). To examine the structural basis for the different roles of these two IBP types, we have solved the first crystal structure of a plant IBP. The 118-residue LpIBP folds as a novel left-handed beta-roll with eight 14- or 15-residue coils and is stabilized by a small hydrophobic core and two internal Asn ladders. The ice-binding site (IBS) is formed by a flat beta-sheet on one surface of the beta-roll. We show that LpIBP binds to both the basal and primary-prism planes of ice, which is the hallmark of hyperactive AFPs. However, the antifreeze activity of LpIBP is less than 10% of that measured for those hyperactive AFPs with convergently evolved beta-solenoid structures. Whereas these hyperactive AFPs have two rows of aligned Thr residues on their IBS, the equivalent arrays in LpIBP are populated by a mixture of Thr, Ser and Val with several side-chain conformations. Substitution of Ser or Val for Thr on the IBS of a hyperactive AFP reduced its antifreeze activity. LpIBP may have evolved an IBS that has low antifreeze activity to avoid damage from rapid ice growth that occurs when temperatures exceed the capacity of AFPs to block ice growth while retaining the ability to inhibit ice recrystallization.
-Antifreeze Protein from Freeze-Tolerant Grass Has a Beta-Roll Fold with an Irregularly Structured Ice-Binding Site.,Middleton AJ, Marshall CB, Faucher F, Bar-Dolev M, Braslavsky I, Campbell RL, Walker VK, Davies PL J Mol Biol. 2012 Jan 28. PMID:22306740<ref>PMID:22306740</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3ult" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Festuca perennis]]
 [[Category: Large Structures]]
-[[Category: Campbell, R L]]
+[[Category: Lolium perenne]]
-[[Category: Davies, P L]]
+[[Category: Campbell RL]]
-[[Category: Faucher, F]]
+[[Category: Davies PL]]
-[[Category: Middleton, A J]]
+[[Category: Faucher F]]
-[[Category: Antifreeze]]
+[[Category: Middleton AJ]]
-[[Category: Antifreeze protein]]
-[[Category: Beta-roll]]
-[[Category: Beta-solenoid]]
-[[Category: Extracellular]]
-[[Category: Ice]]
-[[Category: Ice-binding]]

3ult

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Crystal structure of an ice-binding protein from the perennial ryegrass, Lolium perenne

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