2nwc: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==A 3.02 angstrom crystal structure of wild-type apo GroEL in a monoclinic space group== | ==A 3.02 angstrom crystal structure of wild-type apo GroEL in a monoclinic space group== | ||
<StructureSection load='2nwc' size='340' side='right' caption='[[2nwc]], [[Resolution|resolution]] 3.02Å' scene=''> | <StructureSection load='2nwc' size='340' side='right'caption='[[2nwc]], [[Resolution|resolution]] 3.02Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2nwc]] is a 14 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2nwc]] is a 14 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=2NWC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NWC FirstGlance]. <br> | ||
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">groL, groEL ([ | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">groL, groEL ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Chaperonin_ATPase Chaperonin ATPase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.9 3.6.4.9] </span></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=2nwc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nwc OCA], [https://pdbe.org/2nwc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2nwc RCSB], [https://www.ebi.ac.uk/pdbsum/2nwc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2nwc ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/CH60_ECOUT CH60_ECOUT]] Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (By similarity). | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 31: | Line 31: | ||
==See Also== | ==See Also== | ||
*[[Chaperonin|Chaperonin]] | *[[Chaperonin 3D structures|Chaperonin 3D structures]] | ||
*[[Heat Shock | *[[Heat Shock Protein structures|Heat Shock Protein structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 39: | Line 39: | ||
[[Category: Bacillus coli migula 1895]] | [[Category: Bacillus coli migula 1895]] | ||
[[Category: Chaperonin ATPase]] | [[Category: Chaperonin ATPase]] | ||
[[Category: Large Structures]] | |||
[[Category: Kiser, P D]] | [[Category: Kiser, P D]] | ||
[[Category: Lodowski, D T]] | [[Category: Lodowski, D T]] | ||
Revision as of 18:52, 8 June 2021
A 3.02 angstrom crystal structure of wild-type apo GroEL in a monoclinic space groupA 3.02 angstrom crystal structure of wild-type apo GroEL in a monoclinic space group
Structural highlights
Function[CH60_ECOUT] Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedGroEL is a member of the ATP-dependent chaperonin family that promotes the proper folding of many cytosolic bacterial proteins. The structures of GroEL in a variety of different states have been determined using X-ray crystallography and cryo-electron microscopy. In this study, a 3.02 A crystal structure of the native GroEL complex from Escherichia coli is presented. The complex was purified and crystallized in the absence of potassium ions, which allowed evaluation of the structural changes that may occur in response to cognate potassium-ion binding by comparison to the previously determined wild-type GroEL structure (PDB code 1xck), in which potassium ions were observed in all 14 subunits. In general, the structure is similar to the previously determined wild-type GroEL crystal structure with some differences in regard to temperature-factor distribution. Purification, crystallization and structure determination of native GroEL from Escherichia coli lacking bound potassium ions.,Kiser PD, Lodowski DT, Palczewski K Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Jun 1;63(Pt, 6):457-61. Epub 2007 May 5. PMID:17554162[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||