4v43
From Proteopedia
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==Structural and mechanistic basis for allostery in the bacterial chaperonin GroEL== | ==Structural and mechanistic basis for allostery in the bacterial chaperonin GroEL== | ||
| - | <StructureSection load='4v43' size='340' side='right' caption='[[4v43]], [[Resolution|resolution]] 3.52Å' scene=''> | + | <StructureSection load='4v43' size='340' side='right'caption='[[4v43]], [[Resolution|resolution]] 3.52Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[4v43]] is a 28 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. This structure supersedes | + | <table><tr><td colspan='2'>[[4v43]] is a 28 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1j4z 1j4z] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1kpo 1kpo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V43 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4V43 FirstGlance]. <br> |
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1kp8|1kp8]], [[1der|1der]], [[1oel|1oel]], [[1aon|1aon]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1kp8|1kp8]], [[1der|1der]], [[1oel|1oel]], [[1aon|1aon]]</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=4v43 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v43 OCA], [http://pdbe.org/4v43 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4v43 RCSB], [http://www.ebi.ac.uk/pdbsum/4v43 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4v43 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=4v43 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v43 OCA], [http://pdbe.org/4v43 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4v43 RCSB], [http://www.ebi.ac.uk/pdbsum/4v43 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4v43 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| - | {{Large structure}} | ||
== Function == | == 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/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] | ||
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| + | ==See Also== | ||
| + | *[[Chaperonin 3D structures|Chaperonin 3D structures]] | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Bacillus coli migula 1895]] | [[Category: Bacillus coli migula 1895]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Wang, J]] | [[Category: Wang, J]] | ||
[[Category: Allostery]] | [[Category: Allostery]] | ||
[[Category: Chaperone]] | [[Category: Chaperone]] | ||
[[Category: Wild type groel]] | [[Category: Wild type groel]] | ||
Revision as of 10:45, 26 February 2020
Structural and mechanistic basis for allostery in the bacterial chaperonin GroEL
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