1ugm

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{{STRUCTURE_1ugm| PDB=1ugm | SCENE= }}
{{STRUCTURE_1ugm| PDB=1ugm | SCENE= }}
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'''Crystal Structure of LC3'''
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===Crystal Structure of LC3===
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==Overview==
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Microtubule-associated protein light chain 3 (LC3), a mammalian homologue of yeast Atg8, plays an essential role in autophagy, which is involved in the bulk degradation of cytoplasmic components by the lysosomal system. Here, we report the crystal structure of LC3 at 2.05 A resolution with an R-factor of 21.8% and a free R-factor of 24.9%. The structure of LC3, which is similar to those of Golgi-associated ATPase enhancer of 16 kDa (GATE-16) and GABAA receptor-associated protein (GABARAP), contains a ubiquitin core with two alpha helices, alpha1 and alpha2, attached at its N-terminus. Some common and distinct features are observed among these proteins, including the conservation of residues required to form an interaction among alpha1, alpha2 and the ubiquitin core. However, the electrostatic potential surfaces of these helices differ, implicating particular roles to select specific binding partners. Hydrophobic patches on the ubiquitin core of LC3, GABARAP and GATE-16 are well conserved and are similar to the E1 binding surface of ubiquitin and NEDD8. Therefore, we propose that the hydrophobic patch is a binding surface for mammalian Atg7 similar to a ubiquitin-like conjugation system. We also propose the functional implications of the ubiquitin fold as a recognition module of target proteins.
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{{ABSTRACT_PUBMED_15265004}}
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
The crystal structure of microtubule-associated protein light chain 3, a mammalian homologue of Saccharomyces cerevisiae Atg8., Sugawara K, Suzuki NN, Fujioka Y, Mizushima N, Ohsumi Y, Inagaki F, Genes Cells. 2004 Jul;9(7):611-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15265004 15265004]
The crystal structure of microtubule-associated protein light chain 3, a mammalian homologue of Saccharomyces cerevisiae Atg8., Sugawara K, Suzuki NN, Fujioka Y, Mizushima N, Ohsumi Y, Inagaki F, Genes Cells. 2004 Jul;9(7):611-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15265004 15265004]
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Crystallization and preliminary X-ray analysis of LC3-I., Sugawara K, Suzuki NN, Fujioka Y, Mizushima N, Ohsumi Y, Inagaki F, Acta Crystallogr D Biol Crystallogr. 2003 Aug;59(Pt 8):1464-5. Epub 2003, Jul 23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12876352 12876352]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Autophagy]]
[[Category: Autophagy]]
[[Category: Lc3]]
[[Category: Lc3]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:12:13 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 04:42:53 2008''

Revision as of 01:42, 28 July 2008

Image:1ugm.png

Template:STRUCTURE 1ugm

Crystal Structure of LC3

Template:ABSTRACT PUBMED 15265004

About this Structure

1UGM is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

The crystal structure of microtubule-associated protein light chain 3, a mammalian homologue of Saccharomyces cerevisiae Atg8., Sugawara K, Suzuki NN, Fujioka Y, Mizushima N, Ohsumi Y, Inagaki F, Genes Cells. 2004 Jul;9(7):611-8. PMID:15265004

Crystallization and preliminary X-ray analysis of LC3-I., Sugawara K, Suzuki NN, Fujioka Y, Mizushima N, Ohsumi Y, Inagaki F, Acta Crystallogr D Biol Crystallogr. 2003 Aug;59(Pt 8):1464-5. Epub 2003, Jul 23. PMID:12876352

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