2wfw
From Proteopedia
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| - | <StructureSection load='2wfw' size='340' side='right' caption='[[2wfw]], [[Resolution|resolution]] 1.60Å' scene=''> | + | ==Structure and activity of the N-terminal substrate recognition domains in proteasomal ATPases - The Arc domain structure== |
| + | <StructureSection load='2wfw' size='340' side='right'caption='[[2wfw]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2wfw]] is a 3 chain structure with sequence from [ | + | <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><td class="sblockLbl"><b> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6Å</td></tr> |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <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> | + | </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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wf/2wfw_consurf.spt"</scriptWhenChecked> | + | <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> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </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/ | + | </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="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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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> | 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 | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
</div> | </div> | ||
| + | <div class="pdbe-citations 2wfw" style="background-color:#fffaf0;"></div> | ||
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| + | ==See Also== | ||
| + | *[[ATPase 3D structures|ATPase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Rhodococcus erythropolis]] | [[Category: Rhodococcus erythropolis]] | ||
| - | [[Category: Djuranovic | + | [[Category: Djuranovic S]] |
| - | [[Category: Habeck | + | [[Category: Habeck M]] |
| - | [[Category: Hartmann | + | [[Category: Hartmann MD]] |
| - | [[Category: Lupas | + | [[Category: Lupas AN]] |
| - | [[Category: Martin | + | [[Category: Martin J]] |
| - | [[Category: Ursinus | + | [[Category: Ursinus A]] |
| - | [[Category: Zeth | + | [[Category: Zeth K]] |
| - | [[Category: Zwickl | + | [[Category: Zwickl P]] |
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Current revision
Structure and activity of the N-terminal substrate recognition domains in proteasomal ATPases - The Arc domain structure
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