1n4i

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(New page: 200px<br /><applet load="1n4i" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n4i" /> '''Solution structure of spruce budworm antifre...)
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[[Image:1n4i.jpg|left|200px]]<br /><applet load="1n4i" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1n4i" />
 
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'''Solution structure of spruce budworm antifreeze protein at 5 degrees celsius'''<br />
 
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==Overview==
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==Solution structure of spruce budworm antifreeze protein at 5 degrees celsius==
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Antifreeze proteins (AFPs) prevent the growth of ice, and are used by some, organisms that live in sub-zero environments for protection against, freezing. All AFPs are thought to function by an adsorption inhibition, process. In order to elucidate the ice-binding mechanism, the structures, of several AFPs have been determined, and have been shown to consist of, different folds. Recently, the first structures of the highly active, insect AFPs have been characterized. These proteins have a beta-helix, structure, which adds yet another fold to the AFP family. The 90-residue, spruce budworm (Choristoneura fumiferana) AFP consists of a beta-helix, with 15 residues per coil. The structure contains two ranks of aligned, threonine residues (known as the TXT motif), which were shown by, mutagenesis experiments to be located in the ice-binding face. In our, previous NMR study of this AFP at 30 degrees C, we found that the TXT face, was not optimally defined because of the broadening of NMR resonances, potentially due to weak oligomerization. We present here a structure of, spruce budworm AFP determined at 5 degrees C, where this broadening is, reduced. In addition, the 1H-15N NMR dynamics of the protein were examined, at 30 degrees C and 5 degrees C. The results show that the spruce budworm, AFP is more structured at 5 degrees C, and support the general observation, that AFPs become more rigid as the temperature is lowered.
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<StructureSection load='1n4i' size='340' side='right'caption='[[1n4i]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1n4i]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Choristoneura_fumiferana Choristoneura fumiferana]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N4I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1N4I FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 25 models</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1n4i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n4i OCA], [https://pdbe.org/1n4i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n4i RCSB], [https://www.ebi.ac.uk/pdbsum/1n4i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n4i ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q9GTP0_CHOFU Q9GTP0_CHOFU]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/n4/1n4i_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1n4i ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Antifreeze proteins (AFPs) prevent the growth of ice, and are used by some organisms that live in sub-zero environments for protection against freezing. All AFPs are thought to function by an adsorption inhibition process. In order to elucidate the ice-binding mechanism, the structures of several AFPs have been determined, and have been shown to consist of different folds. Recently, the first structures of the highly active insect AFPs have been characterized. These proteins have a beta-helix structure, which adds yet another fold to the AFP family. The 90-residue spruce budworm (Choristoneura fumiferana) AFP consists of a beta-helix with 15 residues per coil. The structure contains two ranks of aligned threonine residues (known as the TXT motif), which were shown by mutagenesis experiments to be located in the ice-binding face. In our previous NMR study of this AFP at 30 degrees C, we found that the TXT face was not optimally defined because of the broadening of NMR resonances potentially due to weak oligomerization. We present here a structure of spruce budworm AFP determined at 5 degrees C, where this broadening is reduced. In addition, the 1H-15N NMR dynamics of the protein were examined at 30 degrees C and 5 degrees C. The results show that the spruce budworm AFP is more structured at 5 degrees C, and support the general observation that AFPs become more rigid as the temperature is lowered.
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==About this Structure==
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Spruce budworm antifreeze protein: changes in structure and dynamics at low temperature.,Graether SP, Gagne SM, Spyracopoulos L, Jia Z, Davies PL, Sykes BD J Mol Biol. 2003 Apr 11;327(5):1155-68. PMID:12662938<ref>PMID:12662938</ref>
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1N4I is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Choristoneura_fumiferana Choristoneura fumiferana]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1N4I OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Spruce budworm antifreeze protein: changes in structure and dynamics at low temperature., Graether SP, Gagne SM, Spyracopoulos L, Jia Z, Davies PL, Sykes BD, J Mol Biol. 2003 Apr 11;327(5):1155-68. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12662938 12662938]
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</div>
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[[Category: Choristoneura fumiferana]]
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<div class="pdbe-citations 1n4i" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Davies, P.L.]]
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[[Category: Gagne, S.M.]]
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[[Category: Graether, S.P.]]
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[[Category: Jia, Z.]]
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[[Category: Spyracopoulos, L.]]
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[[Category: Sykes, B.D.]]
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[[Category: antifreeze protein]]
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[[Category: beta-helix]]
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[[Category: ice]]
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[[Category: insect]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 22:33:10 2007''
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==See Also==
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*[[Antifreeze protein 3D structures|Antifreeze protein 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Choristoneura fumiferana]]
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[[Category: Large Structures]]
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[[Category: Davies PL]]
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[[Category: Gagne SM]]
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[[Category: Graether SP]]
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[[Category: Jia Z]]
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[[Category: Spyracopoulos L]]
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[[Category: Sykes BD]]

Current revision

Solution structure of spruce budworm antifreeze protein at 5 degrees celsius

PDB ID 1n4i

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