1l0s: Difference between revisions
Jump to navigation
Jump to search
New page: left|200px<br /><applet load="1l0s" size="450" color="white" frame="true" align="right" spinBox="true" caption="1l0s, resolution 2.30Å" /> '''Choristoneura fumife... |
No edit summary |
||
| (17 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
== | ==Choristoneura fumiferana (spruce budworm) antifreeze protein isoform 337== | ||
Reported here is the 2.3 A resolution crystal structure of spruce budworm | <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. | |||
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> | |||
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> | |||
==See Also== | |||
*[[Antifreeze protein 3D structures|Antifreeze protein 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Choristoneura fumiferana]] | [[Category: Choristoneura fumiferana]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Davies | [[Category: Davies PL]] | ||
[[Category: Jia | [[Category: Jia Z]] | ||
[[Category: Leinala | [[Category: Leinala EK]] | ||
Latest revision as of 03:11, 21 November 2024
Choristoneura fumiferana (spruce budworm) antifreeze protein isoform 337Choristoneura fumiferana (spruce budworm) antifreeze protein isoform 337
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedReported 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
| ||||||||||||||||||