4pko: Difference between revisions
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==Crystal structure of the Football-shaped GroEL-GroES2-(ADPBeFx)14 complex== | ==Crystal structure of the Football-shaped GroEL-GroES2-(ADPBeFx)14 complex== | ||
<StructureSection load='4pko' size='340' side='right' caption='[[4pko]], [[Resolution|resolution]] 3.84Å' scene=''> | <StructureSection load='4pko' size='340' side='right'caption='[[4pko]], [[Resolution|resolution]] 3.84Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4pko]] is a 28 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PKO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PKO FirstGlance]. <br> | <table><tr><td colspan='2'>[[4pko]] is a 28 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PKO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PKO 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> | </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> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4pkn|4pkn]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4pkn|4pkn]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">groEL, groL, mopA, BN17_41231, BU34_16740, ECs5124, LF82_0923 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895]), groS, groES, mopB, BN17_41221, BU34_16745, ECs5123, LF82_0924 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr> | |||
<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=4pko FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pko OCA], [http://pdbe.org/4pko PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4pko RCSB], [http://www.ebi.ac.uk/pdbsum/4pko PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4pko ProSAT]</span></td></tr> | <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=4pko FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pko OCA], [http://pdbe.org/4pko PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4pko RCSB], [http://www.ebi.ac.uk/pdbsum/4pko PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4pko ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/Q548M1_ECOLX Q548M1_ECOLX]] Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (By similarity).[RuleBase:RU000419][HAMAP-Rule:MF_00600] [[http://www.uniprot.org/uniprot/Q7BGE6_ECOLX Q7BGE6_ECOLX]] Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter (By similarity).[SAAS:SAAS018369_004_006304][RuleBase:RU000535][HAMAP-Rule:MF_00580] | [[http://www.uniprot.org/uniprot/Q548M1_ECOLX Q548M1_ECOLX]] Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (By similarity).[RuleBase:RU000419][HAMAP-Rule:MF_00600] [[http://www.uniprot.org/uniprot/Q7BGE6_ECOLX Q7BGE6_ECOLX]] Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter (By similarity).[SAAS:SAAS018369_004_006304][RuleBase:RU000535][HAMAP-Rule:MF_00580] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Bacillus coli migula 1895]] | |||
[[Category: Large Structures]] | |||
[[Category: Fei, X]] | [[Category: Fei, X]] | ||
[[Category: Laronde-Leblanc, N]] | [[Category: Laronde-Leblanc, N]] | ||
Revision as of 11:13, 17 April 2019
Crystal structure of the Football-shaped GroEL-GroES2-(ADPBeFx)14 complexCrystal structure of the Football-shaped GroEL-GroES2-(ADPBeFx)14 complex
Structural highlights
Function[Q548M1_ECOLX] Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (By similarity).[RuleBase:RU000419][HAMAP-Rule:MF_00600] [Q7BGE6_ECOLX] Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter (By similarity).[SAAS:SAAS018369_004_006304][RuleBase:RU000535][HAMAP-Rule:MF_00580] Publication Abstract from PubMedThe GroE chaperonins assist substrate protein (SP) folding by cycling through several conformational states. With each cycle the SP is, in turn, captured, unfolded, briefly encapsulated (t1/2 approximately 1 s), and released by the chaperonin complex. The protein-folding functional form is the US-football-shaped GroEL:GroES2 complex. We report structures of two such "football" complexes to approximately 3.7-A resolution; one is empty whereas the other contains encapsulated SP in both chambers. Although encapsulated SP is not visible on the electron density map, using calibrated FRET and order-of-addition experiments we show that owing to SP-catalyzed ADP/ATP exchange both chambers of the football complex encapsulate SP efficiently only if the binding of SP precedes that of ATP. The two rings of GroEL thus behave as a parallel processing machine, rather than functioning alternately. Compared with the bullet-shaped GroEL:GroES1 complex, the GroEL:GroES2 football complex differs conformationally at the GroEL-GroES interface and also at the interface between the two GroEL rings. We propose that the electrostatic interactions between the epsilon-NH3+ of K105 of helix D in one ring with the negatively charged carboxyl oxygen of A109 at the carboxyl end of helix D of the other ring provide the structural basis for negative inter-ring cooperativity. Formation and structures of GroEL:GroES2 chaperonin footballs, the protein-folding functional form.,Fei X, Ye X, LaRonde NA, Lorimer GH Proc Natl Acad Sci U S A. 2014 Aug 18. pii: 201412922. PMID:25136110[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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