We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

2wfw

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

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

Structural highlights

2wfw is a 3 chain structure with sequence from Rhodococcus erythropolis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.6Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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]^[1] ^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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.,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^[3]

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

References

↑ Djuranovic S, Hartmann MD, Habeck M, Ursinus A, Zwickl P, Martin J, Lupas AN, Zeth K. Structure and activity of the N-terminal substrate recognition domains in proteasomal ATPases. Mol Cell. 2009 Jun 12;34(5):580-90. Epub 2009 May 28. PMID:19481487 doi:10.1016/j.molcel.2009.04.030
↑ Wolf S, Nagy I, Lupas A, Pfeifer G, Cejka Z, Muller SA, Engel A, De Mot R, Baumeister W. Characterization of ARC, a divergent member of the AAA ATPase family from Rhodococcus erythropolis. J Mol Biol. 1998 Mar 20;277(1):13-25. PMID:9514743 doi:http://dx.doi.org/S0022-2836(97)91589-8
↑ Djuranovic S, Hartmann MD, Habeck M, Ursinus A, Zwickl P, Martin J, Lupas AN, Zeth K. Structure and activity of the N-terminal substrate recognition domains in proteasomal ATPases. Mol Cell. 2009 Jun 12;34(5):580-90. Epub 2009 May 28. PMID:19481487 doi:10.1016/j.molcel.2009.04.030

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2wfw"

@@ Line 3: / Line 3: @@
 <StructureSection load='2wfw' size='340' side='right'caption='[[2wfw]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2wfw]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/"mycobacterium_erythropolis"_gray_and_thornton_1928 "mycobacterium erythropolis" gray and thornton 1928]. 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>
+<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>
-</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>
+</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>
 </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>
+[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]]
@@ Line 34: / Line 35: @@
 __TOC__
 </StructureSection>
-[[Category: Mycobacterium erythropolis gray and thornton 1928]]
 [[Category: Large Structures]]
-[[Category: Djuranovic, S]]
+[[Category: Rhodococcus erythropolis]]
-[[Category: Habeck, M]]
+[[Category: Djuranovic S]]
-[[Category: Hartmann, M D]]
+[[Category: Habeck M]]
-[[Category: Lupas, A N]]
+[[Category: Hartmann MD]]
-[[Category: Martin, J]]
+[[Category: Lupas AN]]
-[[Category: Ursinus, A]]
+[[Category: Martin J]]
-[[Category: Zeth, K]]
+[[Category: Ursinus A]]
-[[Category: Zwickl, P]]
+[[Category: Zeth K]]
-[[Category: Aaa]]
+[[Category: Zwickl P]]
-[[Category: Arc]]
-[[Category: Atp-binding]]
-[[Category: Atp-binding protein]]
-[[Category: Nucleotide-binding]]
-[[Category: Pan]]
-[[Category: Proteasomal atpase]]

2wfw

From Proteopedia

Current revision

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox