2wfw

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (10:12, 9 May 2024) (edit) (undo)
 
(8 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:2wfw.png|left|200px]]
 
-
<!--
+
==Structure and activity of the N-terminal substrate recognition domains in proteasomal ATPases - The Arc domain structure==
-
The line below this paragraph, containing "STRUCTURE_2wfw", creates the "Structure Box" on the page.
+
<StructureSection load='2wfw' size='340' side='right'caption='[[2wfw]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<table><tr><td colspan='2'>[[2wfw]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodococcus_erythropolis Rhodococcus erythropolis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WFW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WFW FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#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=2wfw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wfw OCA], [https://pdbe.org/2wfw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wfw RCSB], [https://www.ebi.ac.uk/pdbsum/2wfw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wfw ProSAT]</span></td></tr>
-
{{STRUCTURE_2wfw| PDB=2wfw | SCENE= }}
+
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/ARC_RHOER ARC_RHOER] ATPase which is responsible for recognizing, binding, unfolding and translocation of pupylated proteins into the bacterial 20S proteasome core particle. May be essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C-termini of the proteasomal ATPase may function like a 'key in a lock' to induce gate opening and therefore regulate proteolysis.[HAMAP-Rule:MF_02112]<ref>PMID:19481487</ref> <ref>PMID:9514743</ref>
 +
== 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/wf/2wfw_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=2wfw ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
The proteasome forms the core of the protein quality control system in archaea and eukaryotes and also occurs in one bacterial lineage, the Actinobacteria. Access to its proteolytic compartment is controlled by AAA ATPases, whose N-terminal domains (N domains) are thought to mediate substrate recognition. The N domains of an archaeal proteasomal ATPase, Archaeoglobus fulgidus PAN, and of its actinobacterial homolog, Rhodococcus erythropolis ARC, form hexameric rings, whose subunits consist of an N-terminal coiled coil and a C-terminal OB domain. In ARC-N, the OB domains are duplicated and form separate rings. PAN-N and ARC-N can act as chaperones, preventing the aggregation of heterologous proteins in vitro, and this activity is preserved in various chimeras, even when these include coiled coils and OB domains from unrelated proteins. The structures suggest a molecular mechanism for substrate processing based on concerted radial motions of the coiled coils relative to the OB rings.
-
===STRUCTURE AND ACTIVITY OF THE N-TERMINAL SUBSTRATE RECOGNITION DOMAINS IN PROTEASOMAL ATPASES - THE ARC DOMAIN STRUCTURE===
+
Structure and activity of the N-terminal substrate recognition domains in proteasomal ATPases.,Djuranovic S, Hartmann MD, Habeck M, Ursinus A, Zwickl P, Martin J, Lupas AN, Zeth K Mol Cell. 2009 Jun 12;34(5):580-90. Epub 2009 May 28. PMID:19481487<ref>PMID:19481487</ref>
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 2wfw" style="background-color:#fffaf0;"></div>
-
<!--
+
==See Also==
-
The line below this paragraph, {{ABSTRACT_PUBMED_19481487}}, adds the Publication Abstract to the page
+
*[[ATPase 3D structures|ATPase 3D structures]]
-
(as it appears on PubMed at http://www.pubmed.gov), where 19481487 is the PubMed ID number.
+
== References ==
-
-->
+
<references/>
-
{{ABSTRACT_PUBMED_19481487}}
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
[[Category: Large Structures]]
-
[[2wfw]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Rhodococcus_erythropolis Rhodococcus erythropolis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WFW OCA].
+
-
 
+
-
==Reference==
+
-
<ref group="xtra">PMID:019481487</ref><references group="xtra"/>
+
[[Category: Rhodococcus erythropolis]]
[[Category: Rhodococcus erythropolis]]
-
[[Category: Djuranovic, S.]]
+
[[Category: Djuranovic S]]
-
[[Category: Habeck, M.]]
+
[[Category: Habeck M]]
-
[[Category: Hartmann, M D.]]
+
[[Category: Hartmann MD]]
-
[[Category: Lupas, A N.]]
+
[[Category: Lupas AN]]
-
[[Category: Martin, J.]]
+
[[Category: Martin J]]
-
[[Category: Ursinus, A.]]
+
[[Category: Ursinus A]]
-
[[Category: Zeth, K.]]
+
[[Category: Zeth K]]
-
[[Category: Zwickl, P.]]
+
[[Category: Zwickl P]]
-
[[Category: Aaa]]
+
-
[[Category: Arc]]
+
-
[[Category: Atp-binding]]
+
-
[[Category: Atp-binding protein]]
+
-
[[Category: Nucleotide-binding]]
+
-
[[Category: Pan]]
+
-
[[Category: Proteasomal atpase]]
+

Current revision

Structure and activity of the N-terminal substrate recognition domains in proteasomal ATPases - The Arc domain structure

PDB ID 2wfw

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/2wfw"
Personal tools