1xi5: Difference between revisions
New page: left|200px<br /><applet load="1xi5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xi5" /> '''Clathrin D6 coat with auxilin J-domain'''<br... |
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[[Image:1xi5.gif|left|200px]]<br /><applet load="1xi5" size=" | [[Image:1xi5.gif|left|200px]]<br /><applet load="1xi5" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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'''Clathrin D6 coat with auxilin J-domain'''<br /> | '''Clathrin D6 coat with auxilin J-domain'''<br /> | ||
==Overview== | ==Overview== | ||
Clathrin-coated pits invaginate from specific membrane compartments and | Clathrin-coated pits invaginate from specific membrane compartments and pinch off as coated vesicles. These vesicles then uncoat rapidly once released. The Hsc70 molecular chaperone effects the uncoating reaction, and is guided to appropriate locations on clathrin lattices by the J-domain-containing co-chaperone molecule auxilin. This raises the question of how a local event such as ATP hydrolysis by Hsc70 can catalyse a global disassembly. Here, we have used electron cryomicroscopy to determine 12-A-resolution structures of in-vitro-assembled clathrin coats in association with a carboxy-terminal fragment of auxilin that contains both the clathrin-binding region and the J domain. We have located the auxilin fragment by computing differences between these structures and those lacking auxilin (described in an accompanying paper). Auxilin binds within the clathrin lattice near contacts between an inward-projecting C-terminal helical tripod and the crossing of two 'ankle' segments; it also contacts the terminal domain of yet another clathrin 'leg'. It therefore recruits Hsc70 to the neighbourhood of a set of critical interactions. Auxilin binding produces a local change in heavy-chain contacts, creating a detectable global distortion of the clathrin coat. We propose a mechanism by which local destabilization of the lattice promotes general uncoating. | ||
==About this Structure== | ==About this Structure== | ||
1XI5 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http:// | 1XI5 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XI5 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Fotin, A.]] | [[Category: Fotin, A.]] | ||
[[Category: Grigorieff, N.]] | [[Category: Grigorieff, N.]] | ||
[[Category: Harrison, S | [[Category: Harrison, S C.]] | ||
[[Category: Kirchhausen, T.]] | [[Category: Kirchhausen, T.]] | ||
[[Category: Walz, T.]] | [[Category: Walz, T.]] | ||
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[[Category: clathrin]] | [[Category: clathrin]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:55:00 2008'' | ||
Revision as of 16:55, 21 February 2008
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Clathrin D6 coat with auxilin J-domain
OverviewOverview
Clathrin-coated pits invaginate from specific membrane compartments and pinch off as coated vesicles. These vesicles then uncoat rapidly once released. The Hsc70 molecular chaperone effects the uncoating reaction, and is guided to appropriate locations on clathrin lattices by the J-domain-containing co-chaperone molecule auxilin. This raises the question of how a local event such as ATP hydrolysis by Hsc70 can catalyse a global disassembly. Here, we have used electron cryomicroscopy to determine 12-A-resolution structures of in-vitro-assembled clathrin coats in association with a carboxy-terminal fragment of auxilin that contains both the clathrin-binding region and the J domain. We have located the auxilin fragment by computing differences between these structures and those lacking auxilin (described in an accompanying paper). Auxilin binds within the clathrin lattice near contacts between an inward-projecting C-terminal helical tripod and the crossing of two 'ankle' segments; it also contacts the terminal domain of yet another clathrin 'leg'. It therefore recruits Hsc70 to the neighbourhood of a set of critical interactions. Auxilin binding produces a local change in heavy-chain contacts, creating a detectable global distortion of the clathrin coat. We propose a mechanism by which local destabilization of the lattice promotes general uncoating.
About this StructureAbout this Structure
1XI5 is a Protein complex structure of sequences from Bos taurus. Full crystallographic information is available from OCA.
ReferenceReference
Structure of an auxilin-bound clathrin coat and its implications for the mechanism of uncoating., Fotin A, Cheng Y, Grigorieff N, Walz T, Harrison SC, Kirchhausen T, Nature. 2004 Dec 2;432(7017):649-53. Epub 2004 Oct 24. PMID:15502813
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