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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
9
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pubmed:dateCreated |
2009-5-7
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pubmed:databankReference |
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pubmed:abstractText |
Atg8 is conjugated to phosphatidylethanolamine (PE) by ubiquitin-like conjugation reactions. Atg8 has at least two functions in autophagy: membrane biogenesis and target recognition. Regulation of PE conjugation and deconjugation of Atg8 is crucial for these functions in which Atg4 has a critical function by both processing Atg8 precursors and deconjugating Atg8-PE. Here, we report the crystal structures of catalytically inert human Atg4B (HsAtg4B) in complex with processed and unprocessed forms of LC3, a mammalian orthologue of yeast Atg8. On LC3 binding, the regulatory loop and the N-terminal tail of HsAtg4B undergo large conformational changes. The regulatory loop masking the entrance of the active site of free HsAtg4B is lifted by LC3 Phe119, so that a groove is formed along which the LC3 tail enters the active site. At the same time, the N-terminal tail masking the exit of the active site of HsAtg4B in the free form is detached from the enzyme core and a large flat surface is exposed, which might enable the enzyme to access the membrane-bound LC3-PE.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/19322194-10233150,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19322194-10611955,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19322194-11038174,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19322194-11060023,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19322194-11096062,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19322194-11100732,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19322194-11825910,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19322194-12446702,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19322194-14530254,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19322194-14536056,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19322194-15169837,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19322194-15265004,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19322194-15355958,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19322194-15572765,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19322194-16183633,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19322194-16325851,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19322194-16874098,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19322194-17099698,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19322194-17099700,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19322194-17102583,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19322194-17347651,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19322194-17632063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19322194-18006683,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19322194-18321862,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19322194-18508918,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19322194-18524774,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19322194-19021777,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19322194-8132712,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19322194-8520220,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19322194-9757107
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
1460-2075
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
6
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pubmed:volume |
28
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1341-50
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pubmed:dateRevised |
2010-9-22
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pubmed:meshHeading |
pubmed-meshheading:19322194-Autophagy,
pubmed-meshheading:19322194-Crystallography, X-Ray,
pubmed-meshheading:19322194-Cysteine Endopeptidases,
pubmed-meshheading:19322194-Humans,
pubmed-meshheading:19322194-Microtubule-Associated Proteins,
pubmed-meshheading:19322194-Models, Molecular,
pubmed-meshheading:19322194-Protein Binding,
pubmed-meshheading:19322194-Protein Structure, Secondary,
pubmed-meshheading:19322194-Protein Structure, Tertiary
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pubmed:year |
2009
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pubmed:articleTitle |
The structure of Atg4B-LC3 complex reveals the mechanism of LC3 processing and delipidation during autophagy.
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pubmed:affiliation |
Department of Structural Biology, Graduate School of Pharmaceutical Sciences, Hokkaido University, Sapporo, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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