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==Crystal Structure Analysis of the mini-chaperonin variant with Pro 187 Gly== | ==Crystal Structure Analysis of the mini-chaperonin variant with Pro 187 Gly== | ||
<StructureSection load='3vz7' size='340' side='right' caption='[[3vz7]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='3vz7' size='340' side='right'caption='[[3vz7]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3vz7]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3vz7]] is a 1 chain structure with sequence from [https://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=3VZ7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VZ7 FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3vz6|3vz6]], [[3vz8|3vz8]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3vz6|3vz6]], [[3vz8|3vz8]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">groL, groEL, mopA, b4143, JW4103 ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">groL, groEL, mopA, b4143, JW4103 ([https://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'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3vz7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vz7 OCA], [https://pdbe.org/3vz7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vz7 RCSB], [https://www.ebi.ac.uk/pdbsum/3vz7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vz7 ProSAT]</span></td></tr> | ||
</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: Bacillus coli migula 1895]] | [[Category: Bacillus coli migula 1895]] | ||
[[Category: Large Structures]] | |||
[[Category: Saijo, S]] | [[Category: Saijo, S]] | ||
[[Category: Sato, T]] | [[Category: Sato, T]] |
Revision as of 22:11, 27 July 2022
Crystal Structure Analysis of the mini-chaperonin variant with Pro 187 GlyCrystal Structure Analysis of the mini-chaperonin variant with Pro 187 Gly
Structural highlights
Function[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 |
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