5gjq

From Proteopedia

(Difference between revisions)

Current revision

Structure of the human 26S proteasome bound to USP14-UbAl

5gjq, resolution 4.35Å

Structural highlights

5gjq is a 16 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:	Electron Microscopy, Resolution 4.35Å
Ligands:
Experimental data:	Check to display Experimental Data
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PSA7_HUMAN The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. Plays an important role in the regulation of cell proliferation or cell cycle control, transcriptional regulation, immune and stress response, cell differentiation, and apoptosis. Interacts with some important proteins involved in transcription factor regulation, cell cycle transition, viral replication and even tumor initiation and progression. Inhibits the transactivation function of HIF-1A under both normoxic and hypoxia-mimicking conditions. The interaction with EMAP2 increases the proteasome-mediated HIF-1A degradation under the hypoxic conditions. Plays a role in hepatitis C virus internal ribosome entry site-mediated translation. Mediates nuclear translocation of the androgen receptor (AR) and thereby enhances androgen-mediated transactivation. Promotes MAVS degradation and thereby negatively regulates MAVS-mediated innate immune response.^[1] ^[2] ^[3] ^[4] ^[5]

Publication Abstract from PubMed

We report the cryo-EM structure of the human 26S proteasome at an average resolution of 3.5 A, allowing atomic modeling of 28 subunits in the core particle (CP) and 18 subunits in the regulatory particle (RP). The C-terminal residues of Rpt3 and Rpt5 subunits in the RP can be seen inserted into surface pockets formed between adjacent alpha subunits in the CP. Each of the six Rpt subunits contains a bound nucleotide, and the central gate of the CP alpha-ring is closed despite RP association. The six pore 1 loops in the Rpt ring are arranged similarly to a spiral staircase along the axial channel of substrate transport, which is constricted by the pore 2 loops. We also determined the cryo-EM structure of the human proteasome bound to the deubiquitinating enzyme USP14 at 4.35-A resolution. Together, our structures provide a framework for mechanistic understanding of eukaryotic proteasome function.

An atomic structure of the human 26S proteasome.,Huang X, Luan B, Wu J, Shi Y Nat Struct Mol Biol. 2016 Jul 18. doi: 10.1038/nsmb.3273. PMID:27428775^[6]

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

References

↑ Cho S, Choi YJ, Kim JM, Jeong ST, Kim JH, Kim SH, Ryu SE. Binding and regulation of HIF-1alpha by a subunit of the proteasome complex, PSMA7. FEBS Lett. 2001 Jun 1;498(1):62-6. PMID:11389899
↑ Kruger M, Beger C, Welch PJ, Barber JR, Manns MP, Wong-Staal F. Involvement of proteasome alpha-subunit PSMA7 in hepatitis C virus internal ribosome entry site-mediated translation. Mol Cell Biol. 2001 Dec;21(24):8357-64. PMID:11713272 doi:http://dx.doi.org/10.1128/MCB.21.24.8357-8364.2001
↑ Lin HK, Altuwaijri S, Lin WJ, Kan PY, Collins LL, Chang C. Proteasome activity is required for androgen receptor transcriptional activity via regulation of androgen receptor nuclear translocation and interaction with coregulators in prostate cancer cells. J Biol Chem. 2002 Sep 27;277(39):36570-6. Epub 2002 Jul 15. PMID:12119296 doi:http://dx.doi.org/10.1074/jbc.M204751200
↑ Du H, Huang X, Wang S, Wu Y, Xu W, Li M. PSMA7, a potential biomarker of diseases. Protein Pept Lett. 2009;16(5):486-9. PMID:19442227
↑ Jia Y, Song T, Wei C, Ni C, Zheng Z, Xu Q, Ma H, Li L, Zhang Y, He X, Xu Y, Shi W, Zhong H. Negative regulation of MAVS-mediated innate immune response by PSMA7. J Immunol. 2009 Oct 1;183(7):4241-8. doi: 10.4049/jimmunol.0901646. Epub 2009 Sep, 4. PMID:19734229 doi:http://dx.doi.org/10.4049/jimmunol.0901646
↑ Huang X, Luan B, Wu J, Shi Y. An atomic structure of the human 26S proteasome. Nat Struct Mol Biol. 2016 Jul 18. doi: 10.1038/nsmb.3273. PMID:27428775 doi:http://dx.doi.org/10.1038/nsmb.3273

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/5gjq"

@@ Line 1: / Line 1: @@
 ==Structure of the human 26S proteasome bound to USP14-UbAl==
-<SX load='5gjq' size='340' side='right' viewer='molstar' caption='[[5gjq]], [[Resolution|resolution]] 4.50&Aring;' scene=''>
+<SX load='5gjq' size='340' side='right' viewer='molstar' caption='[[5gjq]], [[Resolution|resolution]] 4.35&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5gjq]] is a 20 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=5GJQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GJQ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5gjq]] is a 16 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=5GJQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GJQ FirstGlance]. <br>
-</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.5&#8491;</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.35&#8491;</td></tr>
 <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=GLZ:AMINO-ACETALDEHYDE'>GLZ</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=5gjq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gjq OCA], [https://pdbe.org/5gjq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5gjq RCSB], [https://www.ebi.ac.uk/pdbsum/5gjq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5gjq ProSAT]</span></td></tr>
 </table>
 == Function ==
-[https://www.uniprot.org/uniprot/PSB6_HUMAN PSB6_HUMAN] The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. This unit is responsible of the peptidyl glutamyl-like activity. May catalyze basal processing of intracellular antigens.
+[https://www.uniprot.org/uniprot/PSA7_HUMAN PSA7_HUMAN] The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. Plays an important role in the regulation of cell proliferation or cell cycle control, transcriptional regulation, immune and stress response, cell differentiation, and apoptosis. Interacts with some important proteins involved in transcription factor regulation, cell cycle transition, viral replication and even tumor initiation and progression. Inhibits the transactivation function of HIF-1A under both normoxic and hypoxia-mimicking conditions. The interaction with EMAP2 increases the proteasome-mediated HIF-1A degradation under the hypoxic conditions. Plays a role in hepatitis C virus internal ribosome entry site-mediated translation. Mediates nuclear translocation of the androgen receptor (AR) and thereby enhances androgen-mediated transactivation. Promotes MAVS degradation and thereby negatively regulates MAVS-mediated innate immune response.<ref>PMID:11389899</ref> <ref>PMID:11713272</ref> <ref>PMID:12119296</ref> <ref>PMID:19442227</ref> <ref>PMID:19734229</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

5gjq

From Proteopedia

Current revision

Structure of the human 26S proteasome bound to USP14-UbAl

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

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