1l0s
From Proteopedia
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| - | [[Image:1l0s.jpg|left|200px]]<br /><applet load="1l0s" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1l0s, resolution 2.30Å" /> | ||
| - | '''Choristoneura fumiferana (spruce budworm) antifreeze protein isoform 337'''<br /> | ||
| - | == | + | ==Choristoneura fumiferana (spruce budworm) antifreeze protein isoform 337== |
| + | <StructureSection load='1l0s' size='340' side='right'caption='[[1l0s]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1l0s]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Choristoneura_fumiferana Choristoneura fumiferana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L0S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1L0S FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=TYI:3,5-DIIODOTYROSINE'>TYI</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=1l0s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l0s OCA], [https://pdbe.org/1l0s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1l0s RCSB], [https://www.ebi.ac.uk/pdbsum/1l0s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1l0s ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q9GTP0_CHOFU Q9GTP0_CHOFU] | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/l0/1l0s_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1l0s ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
Reported here is the 2.3 A resolution crystal structure of spruce budworm (Choristoneura fumiferana) antifreeze protein (CfAFP), solved by single anomalous scattering. The structure reveals an extremely regular left-handed beta-helical platform consisting of 15-amino acid loops with a repetitive Thr-X-Thr motif displayed on one of the helix's three faces. This motif results in a two-dimensional array of threonine residues in an identical orientation to those in the nonhomologous, right-handed beta-helical beetle AFP from Tenebrio molitor (TmAFP). The CfAFP structure led us to reevaluate our ice binding model, and the analysis of three possible modes of docking gives rise to a binding mechanism based on surface complementarity. This general mechanism is applicable to both fish and insect AFPs. | Reported here is the 2.3 A resolution crystal structure of spruce budworm (Choristoneura fumiferana) antifreeze protein (CfAFP), solved by single anomalous scattering. The structure reveals an extremely regular left-handed beta-helical platform consisting of 15-amino acid loops with a repetitive Thr-X-Thr motif displayed on one of the helix's three faces. This motif results in a two-dimensional array of threonine residues in an identical orientation to those in the nonhomologous, right-handed beta-helical beetle AFP from Tenebrio molitor (TmAFP). The CfAFP structure led us to reevaluate our ice binding model, and the analysis of three possible modes of docking gives rise to a binding mechanism based on surface complementarity. This general mechanism is applicable to both fish and insect AFPs. | ||
| - | + | Crystal structure of beta-helical antifreeze protein points to a general ice binding model.,Leinala EK, Davies PL, Jia Z Structure. 2002 May;10(5):619-27. PMID:12015145<ref>PMID:12015145</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1l0s" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Antifreeze protein 3D structures|Antifreeze protein 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Choristoneura fumiferana]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Davies PL]] | ||
| + | [[Category: Jia Z]] | ||
| + | [[Category: Leinala EK]] | ||
Current revision
Choristoneura fumiferana (spruce budworm) antifreeze protein isoform 337
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