3b0a
From Proteopedia
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| - | [[Image:3b0a.jpg|left|200px]] | ||
| - | + | ==Crystal structure of the mouse HOIL1-L-NZF in complex with linear di-ubiquitin== | |
| - | + | <StructureSection load='3b0a' size='340' side='right'caption='[[3b0a]], [[Resolution|resolution]] 1.90Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | or the | + | <table><tr><td colspan='2'>[[3b0a]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3B0A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3B0A FirstGlance]. <br> |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> | |
| - | - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TAM:TRIS(HYDROXYETHYL)AMINOMETHANE'>TAM</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=3b0a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b0a OCA], [https://pdbe.org/3b0a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3b0a RCSB], [https://www.ebi.ac.uk/pdbsum/3b0a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3b0a ProSAT]</span></td></tr> | |
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/UBC_HUMAN UBC_HUMAN] Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling.<ref>PMID:16543144</ref> <ref>PMID:19754430</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The linear ubiquitin chain assembly complex (LUBAC) is a key nuclear factor-kappaB (NF-kappaB) pathway component that produces linear polyubiquitin chains. The HOIL-1L subunit of LUBAC has been shown to bind linear chains; however, detailed structural and functional analyses on the binding between LUBAC and linear chains have not been performed. In this study, we found that the Npl4 zinc finger (NZF) domain of HOIL-1L specifically binds linear polyubiquitin chains and determined the crystal structure of the HOIL-1L NZF domain in complex with linear diubiquitin at 1.7-A resolution. The HOIL-1L NZF domain consists of a zinc-coordinating "NZF core" region and an additional alpha-helical "NZF tail" region. The HOIL-1L NZF core binds both the canonical Ile44-centered hydrophobic surface on the distal ubiquitin and a Phe4-centered hydrophobic patch on the proximal ubiquitin, representing a mechanism for the specific recognition of linear chains. The NZF tail binds the proximal ubiquitin to enhance the binding affinity. These recognition mechanisms were supported by the accompanying in vitro and in vivo structure-based mutagenesis experiments. | ||
| - | + | Specific recognition of linear ubiquitin chains by the Npl4 zinc finger (NZF) domain of the HOIL-1L subunit of the linear ubiquitin chain assembly complex.,Sato Y, Fujita H, Yoshikawa A, Yamashita M, Yamagata A, Kaiser SE, Iwai K, Fukai S Proc Natl Acad Sci U S A. 2011 Dec 20;108(51):20520-5. Epub 2011 Dec 2. PMID:22139374<ref>PMID:22139374</ref> | |
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 3b0a" style="background-color:#fffaf0;"></div> | ||
| - | == | + | ==See Also== |
| - | [[ | + | *[[3D structures of ubiquitin|3D structures of ubiquitin]] |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
| - | [[Category: Fujita | + | [[Category: Fujita H]] |
| - | [[Category: Fukai | + | [[Category: Fukai S]] |
| - | [[Category: Iwai | + | [[Category: Iwai K]] |
| - | [[Category: Kaiser | + | [[Category: Kaiser SE]] |
| - | [[Category: Sato | + | [[Category: Sato Y]] |
| - | [[Category: Yamagata | + | [[Category: Yamagata A]] |
| - | [[Category: Yamashita | + | [[Category: Yamashita M]] |
| - | [[Category: Yoshikawa | + | [[Category: Yoshikawa A]] |
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Current revision
Crystal structure of the mouse HOIL1-L-NZF in complex with linear di-ubiquitin
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Categories: Homo sapiens | Large Structures | Mus musculus | Fujita H | Fukai S | Iwai K | Kaiser SE | Sato Y | Yamagata A | Yamashita M | Yoshikawa A
