2mlz
From Proteopedia
(Difference between revisions)
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| - | ''' | + | ==NMR structure of E. coli Trigger Factor in complex with unfolded PhoA365-471== |
| + | <StructureSection load='2mlz' size='340' side='right' caption='[[2mlz]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2mlz]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MLZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MLZ FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2mly|2mly]], [[2mlx|2mlx]]</td></tr> | ||
| + | <tr><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> | ||
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2mlz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mlz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2mlz RCSB], [http://www.ebi.ac.uk/pdbsum/2mlz PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Molecular chaperones prevent aggregation and misfolding of proteins, but scarcity of structural data has impeded an understanding of the recognition and antiaggregation mechanisms. We report the solution structure, dynamics, and energetics of three trigger factor (TF) chaperone molecules in complex with alkaline phosphatase (PhoA) captured in the unfolded state. Our data show that TF uses multiple sites to bind to several regions of the PhoA substrate protein primarily through hydrophobic contacts. Nuclear magnetic resonance (NMR) relaxation experiments show that TF interacts with PhoA in a highly dynamic fashion, but as the number and length of the PhoA regions engaged by TF increase, a more stable complex gradually emerges. Multivalent binding keeps the substrate protein in an extended, unfolded conformation. The results show how molecular chaperones recognize unfolded polypeptides and, by acting as unfoldases and holdases, prevent the aggregation and premature (mis)folding of unfolded proteins. | ||
| - | + | Structural basis for protein antiaggregation activity of the trigger factor chaperone.,Saio T, Guan X, Rossi P, Economou A, Kalodimos CG Science. 2014 May 9;344(6184):1250494. doi: 10.1126/science.1250494. PMID:24812405<ref>PMID:24812405</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Peptidylprolyl isomerase]] | ||
| + | [[Category: Economou, A.]] | ||
| + | [[Category: Guan, X.]] | ||
| + | [[Category: Kalodimos, C G.]] | ||
| + | [[Category: Rossi, P.]] | ||
| + | [[Category: Saio, T.]] | ||
| + | [[Category: Chaperone]] | ||
| + | [[Category: Molecular chaperone]] | ||
| + | [[Category: Unfolded protein]] | ||
Revision as of 09:06, 21 May 2014
NMR structure of E. coli Trigger Factor in complex with unfolded PhoA365-471
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