1o06: Difference between revisions
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[[ | ==Crystal structure of the Vps27p Ubiquitin Interacting Motif (UIM)== | ||
<StructureSection load='1o06' size='340' side='right' caption='[[1o06]], [[Resolution|resolution]] 1.45Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1o06]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O06 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1O06 FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1o06 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o06 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1o06 RCSB], [http://www.ebi.ac.uk/pdbsum/1o06 PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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<ref>PMID:12750381</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
< | |||
[[Category: Alam, S L.]] | [[Category: Alam, S L.]] | ||
[[Category: Fisher, R D.]] | [[Category: Fisher, R D.]] | ||
Revision as of 10:09, 9 June 2014
Crystal structure of the Vps27p Ubiquitin Interacting Motif (UIM)Crystal structure of the Vps27p Ubiquitin Interacting Motif (UIM)
Structural highlights
Publication Abstract from PubMedUbiquitylation 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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