5a0q

From Proteopedia

(Difference between revisions)

Current revision

Cryo-EM reveals the conformation of a substrate analogue in the human 20S proteasome core

5a0q, resolution 3.50Å

Structural highlights

5a0q is a 20 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 3.5Å
Ligands:
Experimental data:	Check to display Experimental Data
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PSA3_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. Binds to the C-terminus of CDKN1A and thereby mediates its degradation. Negatively regulates the membrane trafficking of the cell-surface thromboxane A2 receptor (TBXA2R) isoform 2.^[1] ^[2]

Publication Abstract from PubMed

The proteasome is a highly regulated protease complex fundamental for cell homeostasis and controlled cell cycle progression. It functions by removing a wide range of specifically tagged proteins, including key cellular regulators. Here we present the structure of the human 20S proteasome core bound to a substrate analogue inhibitor molecule, determined by electron cryo-microscopy (cryo-EM) and single-particle analysis at a resolution of around 3.5 A. Our map allows the building of protein coordinates as well as defining the location and conformation of the inhibitor at the different active sites. These results open new prospects to tackle the proteasome functional mechanisms. Moreover, they also further demonstrate that cryo-EM is emerging as a realistic approach for general structural studies of protein-ligand interactions.

Cryo-EM reveals the conformation of a substrate analogue in the human 20S proteasome core.,da Fonseca PC, Morris EP Nat Commun. 2015 Jul 2;6:7573. doi: 10.1038/ncomms8573. PMID:26133119^[3]

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

References

↑ Touitou R, Richardson J, Bose S, Nakanishi M, Rivett J, Allday MJ. A degradation signal located in the C-terminus of p21WAF1/CIP1 is a binding site for the C8 alpha-subunit of the 20S proteasome. EMBO J. 2001 May 15;20(10):2367-75. PMID:11350925 doi:http://dx.doi.org/10.1093/emboj/20.10.2367
↑ Sasaki M, Sukegawa J, Miyosawa K, Yanagisawa T, Ohkubo S, Nakahata N. Low expression of cell-surface thromboxane A2 receptor beta-isoform through the negative regulation of its membrane traffic by proteasomes. Prostaglandins Other Lipid Mediat. 2007 Jun;83(4):237-49. Epub 2006 Dec 27. PMID:17499743 doi:http://dx.doi.org/10.1016/j.prostaglandins.2006.12.001
↑ da Fonseca PC, Morris EP. Cryo-EM reveals the conformation of a substrate analogue in the human 20S proteasome core. Nat Commun. 2015 Jul 2;6:7573. doi: 10.1038/ncomms8573. PMID:26133119 doi:http://dx.doi.org/10.1038/ncomms8573

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/5a0q"

Categories: Homo sapiens | Large Structures | Morris EP | DaFonseca PCA

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5a0q is ON HOLD
+==Cryo-EM reveals the conformation of a substrate analogue in the human 20S proteasome core==
+<SX load='5a0q' size='340' side='right' viewer='molstar' caption='[[5a0q]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5a0q]] 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=5A0Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5A0Q 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]] 3.5&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=KNM:ADA-(AHX)3-(LEU)3-VINYL+SULFONE'>KNM</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=5a0q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a0q OCA], [https://pdbe.org/5a0q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5a0q RCSB], [https://www.ebi.ac.uk/pdbsum/5a0q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5a0q ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/PSA3_HUMAN PSA3_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. Binds to the C-terminus of CDKN1A and thereby mediates its degradation. Negatively regulates the membrane trafficking of the cell-surface thromboxane A2 receptor (TBXA2R) isoform 2.<ref>PMID:11350925</ref> <ref>PMID:17499743</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The proteasome is a highly regulated protease complex fundamental for cell homeostasis and controlled cell cycle progression. It functions by removing a wide range of specifically tagged proteins, including key cellular regulators. Here we present the structure of the human 20S proteasome core bound to a substrate analogue inhibitor molecule, determined by electron cryo-microscopy (cryo-EM) and single-particle analysis at a resolution of around 3.5 A. Our map allows the building of protein coordinates as well as defining the location and conformation of the inhibitor at the different active sites. These results open new prospects to tackle the proteasome functional mechanisms. Moreover, they also further demonstrate that cryo-EM is emerging as a realistic approach for general structural studies of protein-ligand interactions.
-Authors: daFonseca, P.C.A., Morris, E.P.
+Cryo-EM reveals the conformation of a substrate analogue in the human 20S proteasome core.,da Fonseca PC, Morris EP Nat Commun. 2015 Jul 2;6:7573. doi: 10.1038/ncomms8573. PMID:26133119<ref>PMID:26133119</ref>
-Description: Cryo-EM reveals the conformation of a substrate analogue in the human 20S proteasome core
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Morris, E.P]]
+<div class="pdbe-citations 5a0q" style="background-color:#fffaf0;"></div>
-[[Category: Dafonseca, P.C.A]]
+==See Also==
+*[[Proteasome 3D structures|Proteasome 3D structures]]
+== References ==
+<references/>
+__TOC__
+</SX>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Morris EP]]
+[[Category: DaFonseca PCA]]

5a0q

From Proteopedia

Current revision

Cryo-EM reveals the conformation of a substrate analogue in the human 20S proteasome core

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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