This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

3pr9

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

Structural analysis of protein folding by the Methanococcus jannaschii chaperone FKBP26

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3pr9"

Categories: Large Structures | Methanocaldococcus jannaschii | Hendrickson WA | Martinez-Hackert E

@@ Line 3: / Line 3: @@
 <StructureSection load='3pr9' size='340' side='right'caption='[[3pr9]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
 == Structural highlights ==
-<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>
+<table><tr><td colspan='2'>[[3pr9]] is a 1 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=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"><div style='overflow: auto; max-height: 3em;'>[[3pra|3pra]], [[3prb|3prb]], [[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]] 1.95&#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=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>
 == 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 3pr9" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 27: / Line 16: @@
 __TOC__
 </StructureSection>
-[[Category: Atcc 43067]]
 [[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 protein]]

3pr9

From Proteopedia

Current revision

Structural analysis of protein folding by the Methanococcus jannaschii chaperone FKBP26

Structural highlights

Function

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox