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==NMR structure of E. coli Trigger Factor in complex with unfolded PhoA220-310== | ==NMR structure of E. coli Trigger Factor in complex with unfolded PhoA220-310== | ||
<StructureSection load='2mlx' size='340' side='right' caption='[[2mlx]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | <StructureSection load='2mlx' size='340' side='right'caption='[[2mlx]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2mlx]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2mlx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_str._k-12_substr._mc4100 Escherichia coli str. k-12 substr. mc4100]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MLX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MLX FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2mly|2mly]], [[2mlz|2mlz]]</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;'>[[2mly|2mly]], [[2mlz|2mlz]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tig, BN896_0318 ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tig, BN896_0318 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1403831 Escherichia coli str. K-12 substr. MC4100]), phoA, BN896_0267 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1403831 Escherichia coli str. K-12 substr. MC4100])</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=2mlx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mlx OCA], [https://pdbe.org/2mlx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mlx RCSB], [https://www.ebi.ac.uk/pdbsum/2mlx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mlx ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/U6N325_ECOLI U6N325_ECOLI]] Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation (By similarity).[RuleBase:RU003914] Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase (By similarity).[HAMAP-Rule:MF_00303] | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 22: | Line 22: | ||
==See Also== | ==See Also== | ||
*[[Alkaline phosphatase|Alkaline phosphatase]] | *[[Alkaline phosphatase 3D structures|Alkaline phosphatase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 28: | Line 28: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Escherichia coli str. k-12 substr. mc4100]] | [[Category: Escherichia coli str. k-12 substr. mc4100]] | ||
[[Category: Large Structures]] | |||
[[Category: Peptidylprolyl isomerase]] | [[Category: Peptidylprolyl isomerase]] | ||
[[Category: Economou, A]] | [[Category: Economou, A]] | ||
Revision as of 18:17, 2 June 2021
NMR structure of E. coli Trigger Factor in complex with unfolded PhoA220-310NMR structure of E. coli Trigger Factor in complex with unfolded PhoA220-310
Structural highlights
Function[U6N325_ECOLI] Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation (By similarity).[RuleBase:RU003914] Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase (By similarity).[HAMAP-Rule:MF_00303] Publication Abstract from PubMedMolecular 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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