1z96

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1z96 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z96 OCA], [https://pdbe.org/1z96 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1z96 RCSB], [https://www.ebi.ac.uk/pdbsum/1z96 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1z96 ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

The ubiquitin-pathway associated (UBA) domain is a 40-residue polyubiquitin-binding motif. The Schizosaccharomyces pombe protein Mud1 is an ortholog of the Saccharomyces cerevisiae DNA-damage response protein Ddi1 and binds to K48-linked polyubiquitin through its UBA domain. We have solved the crystal structure of Mud1 UBA at 1.8 angstroms resolution, revealing a canonical three-helical UBA fold. We have probed the interactions of this domain using mutagenesis, surface plasmon resonance, NMR and analytical ultracentrifugation. We show that the ubiquitin-binding surface of Mud1 UBA extends beyond previously recognized motifs and can be functionally dissected into primary and secondary ubiquitin-binding sites. Mutation of Phe330 to alanine, a residue exposed between helices 2 and 3, significantly reduces the affinity of the Mud1 UBA domain for K48-linked polyubiquitin, despite leaving the primary binding surface functionally intact. Moreover, K48-linked diubiquitin binds a single Mud1 UBA domain even in the presence of excess UBA. We therefore propose a mechanism for the recognition of K48-linked polyubiquitin chains by Mud1 in which diubiquitin units are specifically recognized by a single UBA domain.

Mechanism of Lys48-linked polyubiquitin chain recognition by the Mud1 UBA domain.,Trempe JF, Brown NR, Lowe ED, Gordon C, Campbell ID, Noble ME, Endicott JA EMBO J. 2005 Sep 21;24(18):3178-89. Epub 2005 Sep 1. PMID:16138082<ref>PMID:16138082</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

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