6w66

From Proteopedia

(Difference between revisions)

Current revision

The structure of the F64A, S172A mutant Keap1-BTB domain in complex with SKP1-FBXL17

Structural highlights

6w66 is a 3 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 3.21Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SKP1_HUMAN Essential component of the SCF (SKP1-CUL1-F-box protein) ubiquitin ligase complex, which mediates the ubiquitination of proteins involved in cell cycle progression, signal transduction and transcription. In the SCF complex, serves as an adapter that links the F-box protein to CUL1. SCF(BTRC) mediates the ubiquitination of NFKBIA at 'Lys-21' and 'Lys-22'; the degradation frees the associated NFKB1-RELA dimer to translocate into the nucleus and to activate transcription. SCF(Cyclin F) directs ubiquitination of CP110.^[1] ^[2]

Publication Abstract from PubMed

Most quality control pathways target misfolded proteins to prevent toxic aggregation and neurodegeneration(1). Dimerization quality control further improves proteostasis by eliminating complexes of aberrant composition(2), but how it detects incorrect subunits remains unknown. Here we provide structural insight into target selection by SCF-FBXL17, a dimerization-quality-control E3 ligase that ubiquitylates and helps to degrade inactive heterodimers of BTB proteins while sparing functional homodimers. We find that SCF-FBXL17 disrupts aberrant BTB dimers that fail to stabilize an intermolecular beta-sheet around a highly divergent beta-strand of the BTB domain. Complex dissociation allows SCF-FBXL17 to wrap around a single BTB domain, resulting in robust ubiquitylation. SCF-FBXL17 therefore probes both shape and complementarity of BTB domains, a mechanism that is well suited to establish quality control of complex composition for recurrent interaction modules.

Structural basis for dimerization quality control.,Mena EL, Jevtic P, Greber BJ, Gee CL, Lew BG, Akopian D, Nogales E, Kuriyan J, Rape M Nature. 2020 Aug 19. pii: 10.1038/s41586-020-2636-7. doi:, 10.1038/s41586-020-2636-7. PMID:32814905^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Hao B, Zheng N, Schulman BA, Wu G, Miller JJ, Pagano M, Pavletich NP. Structural basis of the Cks1-dependent recognition of p27(Kip1) by the SCF(Skp2) ubiquitin ligase. Mol Cell. 2005 Oct 7;20(1):9-19. PMID:16209941 doi:10.1016/j.molcel.2005.09.003
↑ Li Y, Hao B. Structural basis of dimerization-dependent ubiquitination by the SCF(Fbx4) ubiquitin ligase. J Biol Chem. 2010 Apr 30;285(18):13896-906. Epub 2010 Feb 24. PMID:20181953 doi:10.1074/jbc.M110.111518
↑ Mena EL, Jevtic P, Greber BJ, Gee CL, Lew BG, Akopian D, Nogales E, Kuriyan J, Rape M. Structural basis for dimerization quality control. Nature. 2020 Aug 19. pii: 10.1038/s41586-020-2636-7. doi:, 10.1038/s41586-020-2636-7. PMID:32814905 doi:http://dx.doi.org/10.1038/s41586-020-2636-7

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6w66"

@@ Line 1: / Line 1: @@
-====
+==The structure of the F64A, S172A mutant Keap1-BTB domain in complex with SKP1-FBXL17==
-<StructureSection load='6w66' size='340' side='right'caption='[[6w66]]' scene=''>
+<StructureSection load='6w66' size='340' side='right'caption='[[6w66]], [[Resolution|resolution]] 3.21&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6w66]] is a 3 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=6W66 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6W66 FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6w66 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6w66 OCA], [http://pdbe.org/6w66 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6w66 RCSB], [http://www.ebi.ac.uk/pdbsum/6w66 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6w66 ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.21&#8491;</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=6w66 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6w66 OCA], [https://pdbe.org/6w66 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6w66 RCSB], [https://www.ebi.ac.uk/pdbsum/6w66 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6w66 ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/SKP1_HUMAN SKP1_HUMAN] Essential component of the SCF (SKP1-CUL1-F-box protein) ubiquitin ligase complex, which mediates the ubiquitination of proteins involved in cell cycle progression, signal transduction and transcription. In the SCF complex, serves as an adapter that links the F-box protein to CUL1. SCF(BTRC) mediates the ubiquitination of NFKBIA at 'Lys-21' and 'Lys-22'; the degradation frees the associated NFKB1-RELA dimer to translocate into the nucleus and to activate transcription. SCF(Cyclin F) directs ubiquitination of CP110.<ref>PMID:16209941</ref> <ref>PMID:20181953</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Most quality control pathways target misfolded proteins to prevent toxic aggregation and neurodegeneration(1). Dimerization quality control further improves proteostasis by eliminating complexes of aberrant composition(2), but how it detects incorrect subunits remains unknown. Here we provide structural insight into target selection by SCF-FBXL17, a dimerization-quality-control E3 ligase that ubiquitylates and helps to degrade inactive heterodimers of BTB proteins while sparing functional homodimers. We find that SCF-FBXL17 disrupts aberrant BTB dimers that fail to stabilize an intermolecular beta-sheet around a highly divergent beta-strand of the BTB domain. Complex dissociation allows SCF-FBXL17 to wrap around a single BTB domain, resulting in robust ubiquitylation. SCF-FBXL17 therefore probes both shape and complementarity of BTB domains, a mechanism that is well suited to establish quality control of complex composition for recurrent interaction modules.
+Structural basis for dimerization quality control.,Mena EL, Jevtic P, Greber BJ, Gee CL, Lew BG, Akopian D, Nogales E, Kuriyan J, Rape M Nature. 2020 Aug 19. pii: 10.1038/s41586-020-2636-7. doi:, 10.1038/s41586-020-2636-7. PMID:32814905<ref>PMID:32814905</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 6w66" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Kelch-like protein 3D structures|Kelch-like protein 3D structures]]
+== References ==
+<references/>
 __TOC__
 </StructureSection>
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Z-disk]]
+[[Category: Gee CL]]
+[[Category: Kuriyan J]]
+[[Category: Mena EL]]
+[[Category: Rape M]]

6w66

From Proteopedia

Current revision

The structure of the F64A, S172A mutant Keap1-BTB domain in complex with SKP1-FBXL17

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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