4fjv: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older edit
No edit summary
No edit summary
 
(5 intermediate revisions by the same user not shown)
Line 1: Line 1:
{{STRUCTURE_4fjv|  PDB=4fjv  |  SCENE=  }}
===Crystal Structure of Human Otubain2 and Ubiquitin Complex===


==Function==
==Crystal Structure of Human Otubain2 and Ubiquitin Complex==
[[http://www.uniprot.org/uniprot/OTUB2_HUMAN OTUB2_HUMAN]] Hydrolase that can remove conjugated ubiquitin from proteins in vitro and may therefore play an important regulatory role at the level of protein turnover by preventing degradation. Mediates deubiquitination of both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains, with a preference for 'Lys-63'-linked polyubiquitin chains.<ref>PMID:12704427</ref> <ref>PMID:18954305</ref> [[http://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> 
<StructureSection load='4fjv' size='340' side='right'caption='[[4fjv]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4fjv]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FJV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FJV 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]] 2.047&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NEH:ETHANAMINE'>NEH</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=4fjv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fjv OCA], [https://pdbe.org/4fjv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fjv RCSB], [https://www.ebi.ac.uk/pdbsum/4fjv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fjv ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/OTUB2_HUMAN OTUB2_HUMAN] Hydrolase that can remove conjugated ubiquitin from proteins in vitro and may therefore play an important regulatory role at the level of protein turnover by preventing degradation. Mediates deubiquitination of both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains, with a preference for 'Lys-63'-linked polyubiquitin chains.<ref>PMID:12704427</ref> <ref>PMID:18954305</ref>  


==About this Structure==
==See Also==
[[4fjv]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FJV OCA].
*[[Thioesterase 3D structures|Thioesterase 3D structures]]
 
*[[3D structures of ubiquitin|3D structures of ubiquitin]]
==Reference==
== References ==
<references group="xtra"/><references/>
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Ubiquitinyl hydrolase 1]]
[[Category: Large Structures]]
[[Category: Altun, M.]]
[[Category: Altun M]]
[[Category: David, Y.]]
[[Category: David Y]]
[[Category: Iphofer, A.]]
[[Category: Iphofer A]]
[[Category: Kessler, B M.]]
[[Category: Kessler BM]]
[[Category: Komsany, A.]]
[[Category: Komsany A]]
[[Category: Kramer, H B.]]
[[Category: Kramer HB]]
[[Category: Navon, A.]]
[[Category: Navon A]]
[[Category: Nicholson, B.]]
[[Category: Nicholson B]]
[[Category: Ren, J.]]
[[Category: Ren J]]
[[Category: Stuart, D I.]]
[[Category: Stuart DI]]
[[Category: Ternette, N.]]
[[Category: Ternette N]]
[[Category: Walter, T S.]]
[[Category: Walter TS]]
[[Category: Cleavage specificity]]
[[Category: Cysteine protease]]
[[Category: Deubiquitylation]]
[[Category: Hydrolase]]
[[Category: Nedd8]]
[[Category: Otubain]]
[[Category: Ubiquitin]]

Latest revision as of 18:26, 14 March 2024

Crystal Structure of Human Otubain2 and Ubiquitin ComplexCrystal Structure of Human Otubain2 and Ubiquitin Complex

Structural highlights

4fjv is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.047Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

OTUB2_HUMAN Hydrolase that can remove conjugated ubiquitin from proteins in vitro and may therefore play an important regulatory role at the level of protein turnover by preventing degradation. Mediates deubiquitination of both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains, with a preference for 'Lys-63'-linked polyubiquitin chains.[1] [2]

See Also

References

  1. ↑ Balakirev MY, Tcherniuk SO, Jaquinod M, Chroboczek J. Otubains: a new family of cysteine proteases in the ubiquitin pathway. EMBO Rep. 2003 May;4(5):517-22. PMID:12704427 doi:10.1038/sj.embor.embor824
  2. ↑ Edelmann MJ, Iphofer A, Akutsu M, Altun M, di Gleria K, Kramer HB, Fiebiger E, Dhe-Paganon S, Kessler BM. Structural basis and specificity of human otubain 1-mediated deubiquitination. Biochem J. 2009 Mar 1;418(2):379-90. PMID:18954305 doi:10.1042/BJ20081318

4fjv, resolution 2.05Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=4fjv&oldid=4100784"