1q0v: Difference between revisions
New page: left|200px<br /><applet load="1q0v" size="450" color="white" frame="true" align="right" spinBox="true" caption="1q0v" /> '''Solution Structure of Tandem UIMs of Vps27''... |
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'''Solution Structure of Tandem UIMs of Vps27'''<br /> | '''Solution Structure of Tandem UIMs of Vps27'''<br /> | ||
==Overview== | ==Overview== | ||
Monoubiquitylation is a well-characterized signal for the internalization | Monoubiquitylation is a well-characterized signal for the internalization and sorting of integral membrane proteins to distinct cellular organelles. Recognition and transmission of monoubiquitin signals is mediated by a variety of ubiquitin-binding motifs such as UIM, UBA, UEV, VHS and CUE in endocytic proteins. The yeast Vps27 protein requires two UIMs for efficient interactions with ubiquitin and for sorting cargo into multivesicular bodies. Here we show that the individual UIMs of Vps27 exist as autonomously folded alpha-helices that bind ubiquitin independently, non-cooperatively and with modest affinity. The Vps27 N-terminal UIM engages the Leu8-Ile44-Val70 hydrophobic patch of ubiquitin through a helical surface conserved in UIMs of diverse proteins, including that of the S5a proteasomal regulatory subunit. The Leu8-Ile44-Val70 ubiquitin surface is also the site of interaction for CUE and UBA domains in endocytic proteins, consistent with the view that ubiquitin-binding endocytic proteins act serially on the same monoubiquitylated cargo during transport from cell surface to the lysosome. | ||
==About this Structure== | ==About this Structure== | ||
1Q0V is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http:// | 1Q0V is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q0V OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Hicke, L.]] | [[Category: Hicke, L.]] | ||
[[Category: Kang, R | [[Category: Kang, R S.]] | ||
[[Category: Radhakrishnan, I.]] | [[Category: Radhakrishnan, I.]] | ||
[[Category: Stamenova, S | [[Category: Stamenova, S D.]] | ||
[[Category: Swanson, K | [[Category: Swanson, K A.]] | ||
[[Category: non-interacting alpha-helices]] | [[Category: non-interacting alpha-helices]] | ||
[[Category: stable]] | [[Category: stable]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:34:39 2008'' | ||
Revision as of 15:34, 21 February 2008
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Solution Structure of Tandem UIMs of Vps27
OverviewOverview
Monoubiquitylation is a well-characterized signal for the internalization and sorting of integral membrane proteins to distinct cellular organelles. Recognition and transmission of monoubiquitin signals is mediated by a variety of ubiquitin-binding motifs such as UIM, UBA, UEV, VHS and CUE in endocytic proteins. The yeast Vps27 protein requires two UIMs for efficient interactions with ubiquitin and for sorting cargo into multivesicular bodies. Here we show that the individual UIMs of Vps27 exist as autonomously folded alpha-helices that bind ubiquitin independently, non-cooperatively and with modest affinity. The Vps27 N-terminal UIM engages the Leu8-Ile44-Val70 hydrophobic patch of ubiquitin through a helical surface conserved in UIMs of diverse proteins, including that of the S5a proteasomal regulatory subunit. The Leu8-Ile44-Val70 ubiquitin surface is also the site of interaction for CUE and UBA domains in endocytic proteins, consistent with the view that ubiquitin-binding endocytic proteins act serially on the same monoubiquitylated cargo during transport from cell surface to the lysosome.
About this StructureAbout this Structure
1Q0V is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
ReferenceReference
Solution structure of Vps27 UIM-ubiquitin complex important for endosomal sorting and receptor downregulation., Swanson KA, Kang RS, Stamenova SD, Hicke L, Radhakrishnan I, EMBO J. 2003 Sep 15;22(18):4597-606. PMID:12970172
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