6wrf: Difference between revisions
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==ClpX-ClpP complex bound to GFP-ssrA, recognition complex== | |||
<StructureSection load='6wrf' size='340' side='right'caption='[[6wrf]], [[Resolution|resolution]] 3.14Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6wrf]] is a 14 chain structure with sequence from [https://en.wikipedia.org/wiki/Aequorea_victoria Aequorea victoria] and [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6WRF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6WRF 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]] 3.14Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=AGS:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>AGS</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=6wrf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6wrf OCA], [https://pdbe.org/6wrf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6wrf RCSB], [https://www.ebi.ac.uk/pdbsum/6wrf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6wrf ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/CLPX_ECOLI CLPX_ECOLI] ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. It may bind to the lambda O substrate protein and present it to the ClpP protease in a form that can be recognized and readily hydrolyzed by ClpP. Can perform chaperone functions in the absence of ClpP.[HAMAP-Rule:MF_00175] | |||
==See Also== | |||
*[[Green Fluorescent Protein 3D structures|Green Fluorescent Protein 3D structures]] | |||
*[[Heat Shock Protein structures|Heat Shock Protein structures]] | |||
[[Category: | __TOC__ | ||
</StructureSection> | |||
[[Category: Aequorea victoria]] | |||
[[Category: Escherichia coli K-12]] | |||
[[Category: Large Structures]] | |||
[[Category: Fei X]] | |||
[[Category: Sauer RT]] | |||
Latest revision as of 17:46, 6 March 2024
ClpX-ClpP complex bound to GFP-ssrA, recognition complexClpX-ClpP complex bound to GFP-ssrA, recognition complex
Structural highlights
FunctionCLPX_ECOLI ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. It may bind to the lambda O substrate protein and present it to the ClpP protease in a form that can be recognized and readily hydrolyzed by ClpP. Can perform chaperone functions in the absence of ClpP.[HAMAP-Rule:MF_00175] See Also |
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