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==Crystal Structure Analysis of the Mini-chaperonin variant with Leu 185, Val 186, Pro 187, Arg 188 and Ser 190 replaced with all Gly== | ==Crystal Structure Analysis of the Mini-chaperonin variant with Leu 185, Val 186, Pro 187, Arg 188 and Ser 190 replaced with all Gly== | ||
<StructureSection load='3vz8' size='340' side='right' caption='[[3vz8]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='3vz8' size='340' side='right'caption='[[3vz8]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3vz8]] is a 3 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3vz8]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VZ8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VZ8 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</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=3vz8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vz8 OCA], [https://pdbe.org/3vz8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vz8 RCSB], [https://www.ebi.ac.uk/pdbsum/3vz8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vz8 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://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] | ||
==See Also== | ==See Also== | ||
*[[Chaperonin|Chaperonin]] | *[[Chaperonin 3D structures|Chaperonin 3D structures]] | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Escherichia coli]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Saijo S]] | ||
[[Category: | [[Category: Sato T]] | ||
Latest revision as of 15:42, 8 November 2023
Crystal Structure Analysis of the Mini-chaperonin variant with Leu 185, Val 186, Pro 187, Arg 188 and Ser 190 replaced with all GlyCrystal Structure Analysis of the Mini-chaperonin variant with Leu 185, Val 186, Pro 187, Arg 188 and Ser 190 replaced with all Gly
Structural highlights
FunctionCH60_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] See Also |
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