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1l1i

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(New page: 200px<br /><applet load="1l1i" size="450" color="white" frame="true" align="right" spinBox="true" caption="1l1i" /> '''Solution Structure of the Tenebrio molitor A...)
Current revision (08:05, 3 April 2024) (edit) (undo)
 
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[[Image:1l1i.jpg|left|200px]]<br /><applet load="1l1i" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1l1i" />
 
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'''Solution Structure of the Tenebrio molitor Antifreeze Protein'''<br />
 
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==Overview==
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==Solution Structure of the Tenebrio molitor Antifreeze Protein==
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Antifreeze proteins (AFPs) protect many types of organisms from damage, caused by freezing. They do this by binding to the ice surface, which, causes inhibition of ice crystal growth. However, the molecular mechanism, of ice binding leading to growth inhibition is not well understood. In, this paper, we present the solution structure and backbone NMR relaxation, data of the antifreeze protein from the yellow mealworm beetle Tenebrio, molitor (TmAFP) to study the dynamics in the context of structure. The, full (15)N relaxation analysis was completed at two magnetic field, strengths, 500 and 600 MHz, as well as at two temperatures, 30 and 5, degrees C, to measure the dynamic changes that occur in the protein, backbone at different temperatures. TmAFP is a small, highly, disulfide-bonded, right-handed parallel beta-helix consisting of seven, tandemly repeated 12-amino acid loops. The backbone relaxation data, displays a periodic pattern, which reflects both the 12-amino acid, structural repeat and the highly anisotropic nature of the protein., Analysis of the (15)N relaxation parameters shows that TmAFP is a, well-defined, rigid structure, and the extracted parameters show that, there is similar restricted internal mobility throughout the protein, backbone at both temperatures studied. We conclude that the hydrophobic, rigid binding site may reduce the entropic penalty for the binding of the, protein to ice. The beta-helical fold of the protein provides this, rigidity, as it does not appear to be a consequence of cooling toward a, physiologically relevant temperature.
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<StructureSection load='1l1i' size='340' side='right'caption='[[1l1i]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1l1i]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Tenebrio_molitor Tenebrio molitor]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L1I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1L1I 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</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=1l1i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l1i OCA], [https://pdbe.org/1l1i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1l1i RCSB], [https://www.ebi.ac.uk/pdbsum/1l1i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1l1i ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ANPY1_TENMO ANPY1_TENMO] Contributes to protect body fluid from freezing at subzero temperatures. Lowers the freezing point of the hemolymph by about 2.5 degrees at a concentration of 1 mg/ml. Binds to nascent ice crystals and prevents further growth.<ref>PMID:10471292</ref> <ref>PMID:10833402</ref> <ref>PMID:9285581</ref>
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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/l1/1l1i_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1l1i ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1L1I is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Tenebrio_molitor Tenebrio molitor]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1L1I OCA].
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*[[Antifreeze protein 3D structures|Antifreeze protein 3D structures]]
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== References ==
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==Reference==
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<references/>
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Structure and dynamics of a beta-helical antifreeze protein., Daley ME, Spyracopoulos L, Jia Z, Davies PL, Sykes BD, Biochemistry. 2002 Apr 30;41(17):5515-25. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11969412 11969412]
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__TOC__
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[[Category: Single protein]]
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Tenebrio molitor]]
[[Category: Tenebrio molitor]]
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[[Category: Daley, M.E.]]
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[[Category: Daley ME]]
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[[Category: Davies, P.L.]]
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[[Category: Davies PL]]
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[[Category: Jia, Z.]]
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[[Category: Jia Z]]
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[[Category: Spyracopoulos, L.]]
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[[Category: Spyracopoulos L]]
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[[Category: Sykes, B.D.]]
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[[Category: Sykes BD]]
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[[Category: beta-helix]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 02:18:48 2007''
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Current revision

Solution Structure of the Tenebrio molitor Antifreeze Protein

PDB ID 1l1i

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