1v49
From Proteopedia
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Solution structure of microtubule-associated protein light chain-3
Overview
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
1V49 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Mon Nov 12 19:41:22 2007
