5opx
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of the GroEL mutant A109C in complex with GroES and ADP BeF2== | |
| - | + | <StructureSection load='5opx' size='340' side='right' caption='[[5opx]], [[Resolution|resolution]] 3.64Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[5opx]] is a 28 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OPX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5OPX FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=BEF:BERYLLIUM+TRIFLUORIDE+ION'>BEF</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | |
| - | [[Category: | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5opx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5opx OCA], [http://pdbe.org/5opx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5opx RCSB], [http://www.ebi.ac.uk/pdbsum/5opx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5opx ProSAT]</span></td></tr> |
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/CH60_ECOLI CH60_ECOLI]] Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.[HAMAP-Rule:MF_00600] Essential for the growth of the bacteria and the assembly of several bacteriophages. Also plays a role in coupling between replication of the F plasmid and cell division of the cell.[HAMAP-Rule:MF_00600] [[http://www.uniprot.org/uniprot/CH10_ECOLI CH10_ECOLI]] Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.[HAMAP-Rule:MF_00580] | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Bracher, A]] | ||
| + | [[Category: Hartl, F U]] | ||
| + | [[Category: Hayer-Hartl, M]] | ||
| + | [[Category: Milicic, G]] | ||
| + | [[Category: Shi, Q]] | ||
| + | [[Category: Singh, A K]] | ||
[[Category: Yan, X]] | [[Category: Yan, X]] | ||
| - | [[Category: | + | [[Category: Chaperone]] |
| + | [[Category: Chaperonin]] | ||
Revision as of 08:22, 10 January 2018
Crystal structure of the GroEL mutant A109C in complex with GroES and ADP BeF2
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Categories: Bracher, A | Hartl, F U | Hayer-Hartl, M | Milicic, G | Shi, Q | Singh, A K | Yan, X | Chaperone | Chaperonin
