5n4e - Revision history

OCA at 18:01, 8 November 2023

2023-11-08T18:01:41Z

← Older revision		Revision as of 18:01, 8 November 2023
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	<StructureSection load='5n4e' size='340' side='right'caption='[[5n4e]], [[Resolution\|resolution]] 2.90Å' scene=''>		<StructureSection load='5n4e' size='340' side='right'caption='[[5n4e]], [[Resolution\|resolution]] 2.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[5n4e]] is a 4 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Galerina_marginata Galerina marginata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5N4E OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5N4E FirstGlance]. <br>		<table><tr><td colspan='2'>[[5n4e]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Galerina_marginata Galerina marginata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5N4E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5N4E FirstGlance]. <br>
	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat"~~><scene name~~=~~'pdbligand=GOL:GLYCEROL'>GOL</scene~~></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]] 2.9Å</td></tr>
	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat">~~POPB ([http~~:/~~/www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=109633 Galerina marginata])~~</td></tr>		<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=5n4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n4e OCA], [~~http~~://pdbe.org/5n4e PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5n4e RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5n4e PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5n4e 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=5n4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n4e OCA], [https://pdbe.org/5n4e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5n4e RCSB], [https://www.ebi.ac.uk/pdbsum/5n4e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5n4e ProSAT]</span></td></tr>
	</table>		</table>
			== Function ==
			[https://www.uniprot.org/uniprot/POPB_GALM3 POPB_GALM3] Dual function macrocyclase-peptidase involved in the biosynthesis of the highly toxic amanitin toxin family of macrocycles (PubMed:22202811, PubMed:28866879, PubMed:29051530). Cleaves peptide bonds on the C-terminal side of prolyl residues (PubMed:29051530). The enzyme first removes 10 residues from the N-terminus of a 35-residue substrate (PubMed:29051530). Conformational trapping of the 25 amino-acid peptide forces the enzyme to release this intermediate rather than proceed to macrocyclization (PubMed:29051530). The enzyme rebinds the 25 amino-acid peptide in a different conformation and catalyzes macrocyclization of the N-terminal eight residues (PubMed:28866879, PubMed:29051530).<ref>PMID:22202811</ref> <ref>PMID:28866879</ref> <ref>PMID:29051530</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	[[Category: Galerina marginata]]		[[Category: Galerina marginata]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Czekster~~, C M~~]]		[[Category: Czekster CM]]
	[[Category: Ludewig, H]]		[[Category: Ludewig H]]
	[[Category: McMahon~~, S A~~]]		[[Category: McMahon SA]]
	[[Category: Naismith~~, J H]]~~		[[Category: Naismith JH]]
	~~[[Category: Amanitin biosynthesis]]~~
	~~[[Category: Beta-propeller]]~~
	~~[[Category: Closed form]]~~
	~~[[Category: Hydrolase]]~~
	~~[[Category: Macrocyclase]]~~
	~~[[Category: Peptidase]]~~
	~~[[Category: Prolyl oligopeptidase~~]]

OCA at 06:42, 16 October 2019

2019-10-16T06:42:07Z

← Older revision		Revision as of 06:42, 16 October 2019
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	==Prolyl oligopeptidase B from Galerina marginata bound to 35mer hydrolysis and macrocyclization substrate - H698A mutant==		==Prolyl oligopeptidase B from Galerina marginata bound to 35mer hydrolysis and macrocyclization substrate - H698A mutant==
	<StructureSection load='5n4e' size='340' side='right' caption='[[5n4e]], [[Resolution\|resolution]] 2.90Å' scene=''>		<StructureSection load='5n4e' size='340' side='right'caption='[[5n4e]], [[Resolution\|resolution]] 2.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[5n4e]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Galerina_marginata Galerina marginata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5N4E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5N4E FirstGlance]. <br>		<table><tr><td colspan='2'>[[5n4e]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Galerina_marginata Galerina marginata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5N4E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5N4E FirstGlance]. <br>
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	</StructureSection>		</StructureSection>
	[[Category: Galerina marginata]]		[[Category: Galerina marginata]]
			[[Category: Large Structures]]
	[[Category: Czekster, C M]]		[[Category: Czekster, C M]]
	[[Category: Ludewig, H]]		[[Category: Ludewig, H]]

OCA at 07:38, 8 November 2017

2017-11-08T07:38:25Z

← Older revision		Revision as of 07:38, 8 November 2017
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	<StructureSection load='5n4e' size='340' side='right' caption='[[5n4e]], [[Resolution\|resolution]] 2.90Å' scene=''>		<StructureSection load='5n4e' size='340' side='right' caption='[[5n4e]], [[Resolution\|resolution]] 2.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[5n4e]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5N4E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5N4E FirstGlance]. <br>		<table><tr><td colspan='2'>[[5n4e]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Galerina_marginata Galerina marginata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5N4E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5N4E FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
			<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">POPB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=109633 Galerina marginata])</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=5n4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n4e OCA], [http://pdbe.org/5n4e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5n4e RCSB], [http://www.ebi.ac.uk/pdbsum/5n4e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5n4e ProSAT]</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=5n4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n4e OCA], [http://pdbe.org/5n4e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5n4e RCSB], [http://www.ebi.ac.uk/pdbsum/5n4e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5n4e ProSAT]</span></td></tr>
	</table>		</table>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			Peptide macrocycles are promising therapeutic molecules because they are protease resistant, structurally rigid, membrane permeable, and capable of modulating protein-protein interactions. Here, we report the characterization of the dual function macrocyclase-peptidase enzyme involved in the biosynthesis of the highly toxic amanitin toxin family of macrocycles. The enzyme first removes 10 residues from the N-terminus of a 35-residue substrate. Conformational trapping of the 25 amino-acid peptide forces the enzyme to release this intermediate rather than proceed to macrocyclization. The enzyme rebinds the 25 amino-acid peptide in a different conformation and catalyzes macrocyclization of the N-terminal eight residues. Structures of the enzyme bound to both substrates and biophysical analysis characterize the different binding modes rationalizing the mechanism. Using these insights simpler substrates with only five C-terminal residues were designed, allowing the enzyme to be more effectively exploited in biotechnology.

			Characterization of a dual function macrocyclase enables design and use of efficient macrocyclization substrates.,Czekster CM, Ludewig H, McMahon SA, Naismith JH Nat Commun. 2017 Oct 19;8(1):1045. doi: 10.1038/s41467-017-00862-4. PMID:29051530<ref>PMID:29051530</ref>

			From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
			<div class="pdbe-citations 5n4e" style="background-color:#fffaf0;"></div>
			== References ==
			<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
			[[Category: Galerina marginata]]
	[[Category: Czekster, C M]]		[[Category: Czekster, C M]]
	[[Category: Ludewig, H]]		[[Category: Ludewig, H]]

OCA at 06:25, 1 November 2017

2017-11-01T06:25:49Z

← Older revision		Revision as of 06:25, 1 November 2017
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	~~'''Unreleased structure'''~~

	~~The entry~~ 5n4e is ~~ON HOLD~~		==Prolyl oligopeptidase B from Galerina marginata bound to 35mer hydrolysis and macrocyclization substrate - H698A mutant==
			<StructureSection load='5n4e' size='340' side='right' caption='[[5n4e]], [[Resolution\|resolution]] 2.90Å' scene=''>
	~~Authors~~:		== Structural highlights ==
			<table><tr><td colspan='2'>[[5n4e]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5N4E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5N4E FirstGlance]. <br>
	~~Description~~:		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
	[[Category: ~~Unreleased Structures~~]]		<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=5n4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n4e OCA], [http://pdbe.org/5n4e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5n4e RCSB], [http://www.ebi.ac.uk/pdbsum/5n4e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5n4e ProSAT]</span></td></tr>
			</table>
			__TOC__
			</StructureSection>
			[[Category: Czekster, C M]]
			[[Category: Ludewig, H]]
			[[Category: McMahon, S A]]
			[[Category: Naismith, J H]]
			[[Category: Amanitin biosynthesis]]
			[[Category: Beta-propeller]]
			[[Category: Closed form]]
			[[Category: Hydrolase]]
			[[Category: Macrocyclase]]
			[[Category: Peptidase]]
			[[Category: Prolyl oligopeptidase]]

OCA: Protected "5n4e" [edit=sysop:move=sysop]

2017-03-09T12:02:30Z

Protected "5n4e" [edit=sysop:move=sysop]

← Older revision	Revision as of 12:02, 9 March 2017
(No difference)

OCA: New page: '''Unreleased structure''' The entry 5n4e is ON HOLD Authors: Description: Category: Unreleased Structures

2017-03-09T12:02:28Z

New page: '''Unreleased structure''' The entry 5n4e is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 5n4e is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]