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| | ==Structural analysis of protein folding by the Methanococcus jannaschii chaperone FKBP26== | | ==Structural analysis of protein folding by the Methanococcus jannaschii chaperone FKBP26== |
| - | <StructureSection load='3prb' size='340' side='right' caption='[[3prb]], [[Resolution|resolution]] 2.20Å' scene=''> | + | <StructureSection load='3prb' size='340' side='right'caption='[[3prb]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3prb]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/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">[[3pr9|3pr9]], [[3pra|3pra]], [[3prd|3prd]]</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]] 2.2Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MJ0825 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2190 ATCC 43067])</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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </span></td></tr>
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| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3prb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3prb OCA], [http://pdbe.org/3prb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3prb RCSB], [http://www.ebi.ac.uk/pdbsum/3prb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3prb ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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;">
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| - | == Publication Abstract from PubMed ==
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| - | 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.
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| - | 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>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | <div class="pdbe-citations 3prb" style="background-color:#fffaf0;"></div>
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| | ==See Also== | | ==See Also== |
| - | *[[FK506 binding protein|FK506 binding protein]] | + | *[[FKBP 3D structures|FKBP 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </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]]
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| - | [[Category: Fkbp]]
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| - | [[Category: Isomerase]]
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