1v49: Difference between revisions

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New page: left|200px<br /> <applet load="1v49" size="450" color="white" frame="true" align="right" spinBox="true" caption="1v49" /> '''Solution structure of microtubule-associate...
 
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[[Image:1v49.gif|left|200px]]<br />
<applet load="1v49" size="450" color="white" frame="true" align="right" spinBox="true"
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'''Solution structure of microtubule-associated protein light chain-3'''<br />


==Overview==
==Solution structure of microtubule-associated protein light chain-3==
Microtubule-associated protein (MAP) light chain 3 (LC3) is a human, homologue of yeast Apg8/Aut7/Cvt5 (Atg8), which is essential for, autophagy. MAP-LC3 is cleaved by a cysteine protease to produce LC3-I, which is located in cytosolic fraction. LC3-I, in turn, is converted to, LC3-II through the actions of E1- and E2-like enzymes. LC3-II is, covalently attached to phosphatidylethanolamine on its C terminus, and it, binds tightly to autophagosome membranes. We determined the solution, structure of LC3-I and found that it is divided into N- and C-terminal, subdomains. Additional analysis using a photochemically induced dynamic, nuclear polarization technique also showed that the N-terminal subdomain, of LC3-I makes contact with the surface of the C-terminal subdomain and, that LC3-I adopts a single compact conformation in solution. Moreover, the, addition of dodecylphosphocholine into the LC3-I solution induced chemical, shift perturbations primarily in the C-terminal subdomain, which implies, that the two subdomains have different sensitivities to, dodecylphosphocholine micelles. On the other hand, deletion of the, N-terminal subdomain abolished binding of tubulin and microtubules. Thus, we showed that two subdomains of the LC3-I structure have distinct, functions, suggesting that MAP-LC3 can act as an adaptor protein between, microtubules and autophagosomes.
<StructureSection load='1v49' size='340' side='right'caption='[[1v49]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1v49]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V49 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1V49 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1v49 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v49 OCA], [https://pdbe.org/1v49 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1v49 RCSB], [https://www.ebi.ac.uk/pdbsum/1v49 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1v49 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MLP3B_HUMAN MLP3B_HUMAN] Involved in formation of autophagosomal vacuoles (autophagosomes).
== 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/v4/1v49_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1v49 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Microtubule-associated protein (MAP) light chain 3 (LC3) is a human homologue of yeast Apg8/Aut7/Cvt5 (Atg8), which is essential for autophagy. MAP-LC3 is cleaved by a cysteine protease to produce LC3-I, which is located in cytosolic fraction. LC3-I, in turn, is converted to LC3-II through the actions of E1- and E2-like enzymes. LC3-II is covalently attached to phosphatidylethanolamine on its C terminus, and it binds tightly to autophagosome membranes. We determined the solution structure of LC3-I and found that it is divided into N- and C-terminal subdomains. Additional analysis using a photochemically induced dynamic nuclear polarization technique also showed that the N-terminal subdomain of LC3-I makes contact with the surface of the C-terminal subdomain and that LC3-I adopts a single compact conformation in solution. Moreover, the addition of dodecylphosphocholine into the LC3-I solution induced chemical shift perturbations primarily in the C-terminal subdomain, which implies that the two subdomains have different sensitivities to dodecylphosphocholine micelles. On the other hand, deletion of the N-terminal subdomain abolished binding of tubulin and microtubules. Thus, we showed that two subdomains of the LC3-I structure have distinct functions, suggesting that MAP-LC3 can act as an adaptor protein between microtubules and autophagosomes.


==About this Structure==
Solution structure of microtubule-associated protein light chain 3 and identification of its functional subdomains.,Kouno T, Mizuguchi M, Tanida I, Ueno T, Kanematsu T, Mori Y, Shinoda H, Hirata M, Kominami E, Kawano K J Biol Chem. 2005 Jul 1;280(26):24610-7. Epub 2005 Apr 27. PMID:15857831<ref>PMID:15857831</ref>
1V49 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1V49 OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Solution structure of microtubule-associated protein light chain 3 and identification of its functional subdomains., Kouno T, Mizuguchi M, Tanida I, Ueno T, Kanematsu T, Mori Y, Shinoda H, Hirata M, Kominami E, Kawano K, J Biol Chem. 2005 Jul 1;280(26):24610-7. Epub 2005 Apr 27. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15857831 15857831]
</div>
<div class="pdbe-citations 1v49" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Microtubule-associated protein 3D structures|Microtubule-associated protein 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Kawano, K.]]
[[Category: Kawano K]]
[[Category: Kominami, E.]]
[[Category: Kominami E]]
[[Category: Kouno, T.]]
[[Category: Kouno T]]
[[Category: Mizuguchi, M.]]
[[Category: Mizuguchi M]]
[[Category: Tanida, I.]]
[[Category: Tanida I]]
[[Category: Ueno, T.]]
[[Category: Ueno T]]
[[Category: ubiquitin fold]]
 
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