2mlz: 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=''>
+<StructureSection load='2mlz' size='340' side='right'caption='[[2mlz]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2mlz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli] and [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=2MLZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MLZ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2mlz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12] and [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=2MLZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MLZ 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;'>[[2mly|2mly]], [[2mlx|2mlx]]</div></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
-<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, b0383, JW0374 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=2mlz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mlz OCA], [https://pdbe.org/2mlz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mlz RCSB], [https://www.ebi.ac.uk/pdbsum/2mlz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mlz ProSAT]</span></td></tr>
 </table>
 == 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]
+[https://www.uniprot.org/uniprot/PPB_ECOLI PPB_ECOLI]
-<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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 2mlz" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Alkaline phosphatase 3D structures|Alkaline phosphatase 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Ecoli]]
+[[Category: Escherichia coli K-12]]
-[[Category: Escherichia coli str. k-12 substr. mc4100]]
+[[Category: Escherichia coli str. K-12 substr. MC4100]]
 [[Category: Large Structures]]
-[[Category: Peptidylprolyl isomerase]]
+[[Category: Economou A]]
-[[Category: Economou, A]]
+[[Category: Guan X]]
-[[Category: Guan, X]]
+[[Category: Kalodimos CG]]
-[[Category: Kalodimos, C G]]
+[[Category: Rossi P]]
-[[Category: Rossi, P]]
+[[Category: Saio T]]
-[[Category: Saio, T]]
-[[Category: Chaperone]]
-[[Category: Molecular chaperone]]
-[[Category: Unfolded protein]]