1o06: Difference between revisions
New page: left|200px<br /><applet load="1o06" size="450" color="white" frame="true" align="right" spinBox="true" caption="1o06, resolution 1.45Å" /> '''Crystal structure of... |
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[[Image:1o06.gif|left|200px]]<br /><applet load="1o06" size=" | [[Image:1o06.gif|left|200px]]<br /><applet load="1o06" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1o06, resolution 1.45Å" /> | caption="1o06, resolution 1.45Å" /> | ||
'''Crystal structure of the Vps27p Ubiquitin Interacting Motif (UIM)'''<br /> | '''Crystal structure of the Vps27p Ubiquitin Interacting Motif (UIM)'''<br /> | ||
==Overview== | ==Overview== | ||
Ubiquitylation is used to target proteins into a large number of different | Ubiquitylation is used to target proteins into a large number of different biological processes including proteasomal degradation, endocytosis, virus budding, and vacuolar protein sorting (Vps). Ubiquitylated proteins are typically recognized using one of several different conserved ubiquitin binding modules. Here, we report the crystal structure and ubiquitin binding properties of one such module, the ubiquitin-interacting motif (UIM). We found that UIM peptides from several proteins involved in endocytosis and vacuolar protein sorting including Hrs, Vps27p, Stam1, and Eps15 bound specifically, but with modest affinity (Kd = 0.1-1 mm), to free ubiquitin. Full affinity ubiquitin binding required the presence of conserved acidic patches at the N and C terminus of the UIM, as well as highly conserved central alanine and serine residues. NMR chemical shift perturbation mapping experiments demonstrated that all of these UIM peptides bind to the I44 surface of ubiquitin. The 1.45 A resolution crystal structure of the second yeast Vps27p UIM (Vps27p-2) revealed that the ubiquitin-interacting motif forms an amphipathic helix. Although Vps27p-2 is monomeric in solution, the motif unexpectedly crystallized as an antiparallel four-helix bundle, and the potential biological implications of UIM oligomerization are therefore discussed. | ||
==About this Structure== | ==About this Structure== | ||
1O06 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 1O06 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O06 OCA]. | ||
==Reference== | ==Reference== | ||
Structure and ubiquitin binding of the ubiquitin-interacting motif., Fisher RD, Wang B, Alam SL, Higginson DS, Robinson H, Sundquist WI, Hill CP, J Biol Chem. 2003 Aug 1;278(31):28976-84. Epub 2003 May 14. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12750381 12750381] | Structure and ubiquitin binding of the ubiquitin-interacting motif., Fisher RD, Wang B, Alam SL, Higginson DS, Robinson H, Sundquist WI, Hill CP, J Biol Chem. 2003 Aug 1;278(31):28976-84. Epub 2003 May 14. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12750381 12750381] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Alam, S | [[Category: Alam, S L.]] | ||
[[Category: Fisher, R | [[Category: Fisher, R D.]] | ||
[[Category: Higginson, D | [[Category: Higginson, D S.]] | ||
[[Category: Hill, C | [[Category: Hill, C P.]] | ||
[[Category: Myszka, D.]] | [[Category: Myszka, D.]] | ||
[[Category: Rich, R.]] | [[Category: Rich, R.]] | ||
[[Category: Sundquist, W | [[Category: Sundquist, W I.]] | ||
[[Category: Wang, B.]] | [[Category: Wang, B.]] | ||
[[Category: ZN]] | [[Category: ZN]] | ||
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[[Category: tetramer]] | [[Category: tetramer]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:11:59 2008'' | ||
Revision as of 15:12, 21 February 2008
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Crystal structure of the Vps27p Ubiquitin Interacting Motif (UIM)
OverviewOverview
Ubiquitylation is used to target proteins into a large number of different biological processes including proteasomal degradation, endocytosis, virus budding, and vacuolar protein sorting (Vps). Ubiquitylated proteins are typically recognized using one of several different conserved ubiquitin binding modules. Here, we report the crystal structure and ubiquitin binding properties of one such module, the ubiquitin-interacting motif (UIM). We found that UIM peptides from several proteins involved in endocytosis and vacuolar protein sorting including Hrs, Vps27p, Stam1, and Eps15 bound specifically, but with modest affinity (Kd = 0.1-1 mm), to free ubiquitin. Full affinity ubiquitin binding required the presence of conserved acidic patches at the N and C terminus of the UIM, as well as highly conserved central alanine and serine residues. NMR chemical shift perturbation mapping experiments demonstrated that all of these UIM peptides bind to the I44 surface of ubiquitin. The 1.45 A resolution crystal structure of the second yeast Vps27p UIM (Vps27p-2) revealed that the ubiquitin-interacting motif forms an amphipathic helix. Although Vps27p-2 is monomeric in solution, the motif unexpectedly crystallized as an antiparallel four-helix bundle, and the potential biological implications of UIM oligomerization are therefore discussed.
About this StructureAbout this Structure
1O06 is a Single protein structure of sequence from [1] with as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Structure and ubiquitin binding of the ubiquitin-interacting motif., Fisher RD, Wang B, Alam SL, Higginson DS, Robinson H, Sundquist WI, Hill CP, J Biol Chem. 2003 Aug 1;278(31):28976-84. Epub 2003 May 14. PMID:12750381
Page seeded by OCA on Thu Feb 21 14:11:59 2008