3pr9: Difference between revisions
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<StructureSection load='3pr9' size='340' side='right'caption='[[3pr9]], [[Resolution|resolution]] 1.95Å' scene=''> | <StructureSection load='3pr9' size='340' side='right'caption='[[3pr9]], [[Resolution|resolution]] 1.95Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3pr9]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3pr9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_43067 Atcc 43067]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PR9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PR9 FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3pra|3pra]], [[3prb|3prb]], [[3prd|3prd]]</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;'>[[3pra|3pra]], [[3prb|3prb]], [[3prd|3prd]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MJ0825 ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MJ0825 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2190 ATCC 43067])</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/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </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=3pr9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pr9 OCA], [https://pdbe.org/3pr9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pr9 RCSB], [https://www.ebi.ac.uk/pdbsum/3pr9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pr9 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/FKBP2_METJA FKBP2_METJA]] PPIases accelerate the folding of proteins. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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==See Also== | ==See Also== | ||
*[[ | *[[FKBP 3D structures|FKBP 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 11:51, 25 May 2022
Structural analysis of protein folding by the Methanococcus jannaschii chaperone FKBP26Structural analysis of protein folding by the Methanococcus jannaschii chaperone FKBP26
Structural highlights
Function[FKBP2_METJA] PPIases accelerate the folding of proteins. Publication Abstract from PubMedIn the cell, protein folding is mediated by folding catalysts and chaperones. The two functions are often linked, especially when the catalytic module forms part of a multidomain protein, as in Methanococcus jannaschii peptidyl-prolyl cis/trans isomerase FKBP26. Here, we show that FKBP26 chaperone activity requires both a 50-residue insertion in the catalytic FKBP domain, also called 'Insert-in-Flap' or IF domain, and an 80-residue C-terminal domain. We determined FKBP26 structures from four crystal forms and analyzed chaperone domains in light of their ability to mediate protein-protein interactions. FKBP26 is a crescent-shaped homodimer. We reason that folding proteins are bound inside the large crescent cleft, thus enabling their access to inward-facing peptidyl-prolyl cis/trans isomerase catalytic sites and ipsilateral chaperone domain surfaces. As these chaperone surfaces participate extensively in crystal lattice contacts, we speculate that the observed lattice contacts reflect a proclivity for protein associations and represent substrate interactions by FKBP26 chaperone domains. Finally, we find that FKBP26 is an exceptionally flexible molecule, suggesting a mechanism for nonspecific substrate recognition. Structural Analysis of Protein Folding by the Long-Chain Archaeal Chaperone FKBP26.,Martinez-Hackert E, Hendrickson WA J Mol Biol. 2011 Apr 1;407(3):450-64. Epub 2011 Jan 22. PMID:21262232[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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