1z7q

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (07:05, 23 August 2023) (edit) (undo)
 
(7 intermediate revisions not shown.)
Line 1: Line 1:
-
{{Large structure}}
 
-
{{STRUCTURE_1z7q| PDB=1z7q | SCENE= }}
 
-
===Crystal structure of the 20s proteasome from yeast in complex with the proteasome activator PA26 from Trypanosome brucei at 3.2 angstroms resolution===
 
-
{{ABSTRACT_PUBMED_15916965}}
 
-
==About this Structure==
+
==Crystal structure of the 20s proteasome from yeast in complex with the proteasome activator PA26 from Trypanosome brucei at 3.2 angstroms resolution==
-
[[1z7q]] is a 42 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] and [http://en.wikipedia.org/wiki/Trypanosoma_brucei Trypanosoma brucei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z7Q OCA].
+
<StructureSection load='1z7q' size='340' side='right'caption='[[1z7q]], [[Resolution|resolution]] 3.22&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1z7q]] is a 20 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z7Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Z7Q 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]] 3.22&#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=1z7q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z7q OCA], [https://pdbe.org/1z7q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1z7q RCSB], [https://www.ebi.ac.uk/pdbsum/1z7q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1z7q ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/PSA1_YEAST PSA1_YEAST] The proteasome degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus. It is essential for the regulated turnover of proteins and for the removal of misfolded proteins. The proteasome is a multicatalytic proteinase complex that 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. It has an ATP-dependent proteolytic activity.
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/z7/1z7q_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1z7q ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Proteasomes are cylindrical structures that function in multiple cellular processes by degrading a wide variety of cytosolic and nuclear proteins. Substrate access and product release from the enclosed catalytic chamber occurs through axial pores that are opened by activator complexes. Here, we report high-resolution structures of wild-type and mutant archaeal proteasomes bound to the activator PA26. These structures support the proposal that an ordered open conformation is required for proteolysis and that its formation can be triggered by outward displacement of surrounding residues. The structures and associated biochemical assays reveal the mechanism of binding, which involves an interaction between the PA26 C terminus and a conserved lysine. Surprisingly, biochemical observations implicate an equivalent interaction for the unrelated ATP-dependent activators PAN and PA700.
-
==See Also==
+
The 1.9 A structure of a proteasome-11S activator complex and implications for proteasome-PAN/PA700 interactions.,Forster A, Masters EI, Whitby FG, Robinson H, Hill CP Mol Cell. 2005 May 27;18(5):589-99. PMID:15916965<ref>PMID:15916965</ref>
-
*[[Proteasome|Proteasome]]
+
-
==Reference==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
<ref group="xtra">PMID:015916965</ref><references group="xtra"/>
+
</div>
-
[[Category: Proteasome endopeptidase complex]]
+
<div class="pdbe-citations 1z7q" style="background-color:#fffaf0;"></div>
 +
 
 +
==See Also==
 +
*[[Proteasome 3D structures|Proteasome 3D structures]]
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
-
[[Category: Trypanosoma brucei]]
+
[[Category: Forster A]]
-
[[Category: Forster, A.]]
+
[[Category: Hill CP]]
-
[[Category: Hill, C P.]]
+
[[Category: Whitby FG]]
-
[[Category: Whitby, F G.]]
+
-
[[Category: 20]]
+
-
[[Category: Activator]]
+
-
[[Category: Hydrolase-hydrolase activator complex]]
+
-
[[Category: Multi-catalytic protease]]
+
-
[[Category: Pa26]]
+
-
[[Category: Proteasome]]
+

Current revision

Crystal structure of the 20s proteasome from yeast in complex with the proteasome activator PA26 from Trypanosome brucei at 3.2 angstroms resolution

PDB ID 1z7q

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1z7q"
Personal tools