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<StructureSection load='3prb' size='340' side='right'caption='[[3prb]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='3prb' size='340' side='right'caption='[[3prb]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3prb]] is a 2 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=3PRB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PRB FirstGlance]. <br>
<table><tr><td colspan='2'>[[3prb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PRB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PRB FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3pr9|3pr9]], [[3pra|3pra]], [[3prd|3prd]]</div></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
<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'>[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'>[https://proteopedia.org/fgij/fg.htm?mol=3prb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3prb OCA], [https://pdbe.org/3prb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3prb RCSB], [https://www.ebi.ac.uk/pdbsum/3prb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3prb ProSAT]</span></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=3prb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3prb OCA], [https://pdbe.org/3prb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3prb RCSB], [https://www.ebi.ac.uk/pdbsum/3prb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3prb ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/FKBP2_METJA FKBP2_METJA]] PPIases accelerate the folding of proteins.
[https://www.uniprot.org/uniprot/FKBPL_METJA FKBPL_METJA] Catalyzes the cis-trans isomerization of peptidyl prolyl bonds and accelerates protein folding (By similarity). Also exhibits chaperone-like activity (PubMed:21262232).[UniProtKB:O27197]<ref>PMID:21262232</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
In 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<ref>PMID:21262232</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3prb" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 43067]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Peptidylprolyl isomerase]]
[[Category: Methanocaldococcus jannaschii]]
[[Category: Hendrickson, W A]]
[[Category: Hendrickson WA]]
[[Category: Martinez-Hackert, E]]
[[Category: Martinez-Hackert E]]
[[Category: Chaperone]]
[[Category: Fkbp]]
[[Category: Isomerase]]
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