2mlx - Revision history

OCA at 07:01, 1 May 2024

2024-05-01T07:01:03Z

←Older revision		Revision as of 07:01, 1 May 2024
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	== Structural highlights ==		== Structural highlights ==
	<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>		<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='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>	+	</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='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>
-	<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>
-	<div class="pdbe-citations 2mlx" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Alkaline phosphatase 3D structures\|Alkaline phosphatase 3D structures]]		*[[Alkaline phosphatase 3D structures\|Alkaline phosphatase 3D structures]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 08:01, 8 March 2023

2023-03-08T08:01:07Z

←Older revision		Revision as of 08:01, 8 March 2023
Line 1:		Line 1:

	==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]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<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>	+	<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"><div style='overflow: auto; max-height: 3em;'>[[2mly\|2mly]], [[2mlz\|2mlz]]</div></td></tr>~~	+	</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=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>
-	<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'>[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=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 ==
-	[[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 27:		Line 22:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Escherichia coli str. k-12 substr. ~~mc4100~~]]	+	[[Category: Escherichia coli str. K-12 substr. MC4100]]
	[[Category: Large Structures]]		[[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: Protein complex]]~~	+
-	~~[[Category: Unfolded protein~~]]	+

OCA at 15:17, 2 June 2021

2021-06-02T15:17:07Z

←Older revision		Revision as of 15:17, 2 June 2021
Line 1:		Line 1:

	==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 [~~http~~://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 [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2MLX FirstGlance]. <br>	+	<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 ([~~http~~://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 ([~~http~~://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='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'>[~~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 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'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2mlx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mlx OCA], [~~http~~://pdbe.org/2mlx PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2mlx RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2mlx PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2mlx ProSAT]</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=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 ==
-	[[~~http~~://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/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]]

OCA at 22:48, 9 August 2018

2018-08-09T22:48:19Z

←Older revision		Revision as of 22:48, 9 August 2018
Line 1:		Line 1:
		+
	==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. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MLX FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2mlx]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/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">[[2mly\|2mly]], [[2mlz\|2mlz]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">tig, BN896_0318 ([http://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 ([http://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'>[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 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>
-	<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=2mlx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mlx OCA], [http://pdbe.org/2mlx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2mlx RCSB], [http://www.ebi.ac.uk/pdbsum/2mlx PDBsum]</span></td></tr>	+	<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=2mlx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mlx OCA], [http://pdbe.org/2mlx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2mlx RCSB], [http://www.ebi.ac.uk/pdbsum/2mlx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2mlx ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 25:		Line 27:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Escherichia coli str. k-12 substr. mc4100]]
	[[Category: Peptidylprolyl isomerase]]		[[Category: Peptidylprolyl isomerase]]
	[[Category: Economou, A]]		[[Category: Economou, A]]

OCA at 18:35, 10 September 2015

2015-09-10T18:35:50Z

←Older revision		Revision as of 18:35, 10 September 2015
Line 5:		Line 5:
	</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">[[2mly\|2mly]], [[2mlz\|2mlz]]</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>		<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>
-	<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=2mlx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mlx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2mlx RCSB], [http://www.ebi.ac.uk/pdbsum/2mlx PDBsum]</span></td></tr>	+	<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=2mlx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mlx OCA], [http://pdbe.org/2mlx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2mlx RCSB], [http://www.ebi.ac.uk/pdbsum/2mlx PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 17:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 2mlx" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Alkaline phosphatase\|Alkaline phosphatase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 04:24, 25 December 2014

2014-12-25T04:24:13Z

←Older revision		Revision as of 04:24, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2mlx]] is a 2 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MLX FirstGlance]. <br>		<table><tr><td colspan='2'>[[2mlx]] is a 2 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MLX FirstGlance]. <br>
-	</td></tr><tr><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">[[2mly\|2mly]], [[2mlz\|2mlz]]</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 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>
-	<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=2mlx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mlx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2mlx RCSB], [http://www.ebi.ac.uk/pdbsum/2mlx PDBsum]</span></td></tr>	+	<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=2mlx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mlx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2mlx RCSB], [http://www.ebi.ac.uk/pdbsum/2mlx PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://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 13:		Line 15:
	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>		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 ~~MEDLINEÂ®~~/~~PubMedÂ®~~, a database of the U.S. National Library of Medicine.<br>	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
	== References ==		== References ==
Line 20:		Line 22:
	</StructureSection>		</StructureSection>
	[[Category: Peptidylprolyl isomerase]]		[[Category: Peptidylprolyl isomerase]]
-	[[Category: Economou, A.]]	+	[[Category: Economou, A]]
-	[[Category: Guan, X.]]	+	[[Category: Guan, X]]
-	[[Category: Kalodimos, C G.]]	+	[[Category: Kalodimos, C G]]
-	[[Category: Rossi, P.]]	+	[[Category: Rossi, P]]
-	[[Category: Saio, T.]]	+	[[Category: Saio, T]]
	[[Category: Chaperone]]		[[Category: Chaperone]]
	[[Category: Molecular chaperone]]		[[Category: Molecular chaperone]]
	[[Category: Protein complex]]		[[Category: Protein complex]]
	[[Category: Unfolded protein]]		[[Category: Unfolded protein]]

OCA at 09:04, 21 May 2014

2014-05-21T09:04:15Z

←Older revision		Revision as of 09:04, 21 May 2014
Line 1:		Line 1:
-	'''~~Unreleased~~ structure'''	+	==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=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[2mlx]] is a 2 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MLX FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2mly\|2mly]], [[2mlz\|2mlz]]</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=2mlx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mlx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2mlx RCSB], [http://www.ebi.ac.uk/pdbsum/2mlx 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.

-	~~The entry 2mlx is ON HOLD until Paper Publication~~	+	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>

-	~~Authors: Saio~~, T.~~, Guan, X~~.~~, Rossi, P~~., Economou, A., Kalodimos, C.G.	+	From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~Description~~: ~~NMR structure of E~~. ~~coli Trigger Factor in~~ complex ~~with unfolded PhoA220-310~~	+	== 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: Protein complex]]
		+	[[Category: Unfolded protein]]

OCA at 05:30, 9 April 2014

2014-04-09T05:30:05Z

←Older revision		Revision as of 05:30, 9 April 2014
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 2mlx is ON HOLD	+	The entry 2mlx is ON HOLD until Paper Publication

	Authors: Saio, T., Guan, X., Rossi, P., Economou, A., Kalodimos, C.G.		Authors: Saio, T., Guan, X., Rossi, P., Economou, A., Kalodimos, C.G.

	Description: NMR structure of E. coli Trigger Factor in complex with unfolded PhoA220-310		Description: NMR structure of E. coli Trigger Factor in complex with unfolded PhoA220-310

OCA: Protected "2mlx" [edit=sysop:move=sysop]

2014-03-12T11:32:47Z

Protected "2mlx" [edit=sysop:move=sysop]

←Older revision

Revision as of 11:32, 12 March 2014

OCA: New page: '''Unreleased structure''' The entry 2mlx is ON HOLD Authors: Saio, T., Guan, X., Rossi, P., Economou, A., Kalodimos, C.G. Description: NMR structure of E. coli Trigger Factor in compl...

2014-03-12T11:32:46Z

New page: '''Unreleased structure''' The entry 2mlx is ON HOLD Authors: Saio, T., Guan, X., Rossi, P., Economou, A., Kalodimos, C.G. Description: NMR structure of E. coli Trigger Factor in compl...

New page

'''Unreleased structure'''

The entry 2mlx is ON HOLD

Authors: Saio, T., Guan, X., Rossi, P., Economou, A., Kalodimos, C.G.

Description: NMR structure of E. coli Trigger Factor in complex with unfolded PhoA220-310