OCA at 12:36, 24 January 2024

OCA — Wed, 24 Jan 2024 12:36:24 GMT

←Older revision		Revision as of 12:36, 24 January 2024
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	==Crystal Structure of the Homospermidine Synthase (HSS) variant W229A from Blastochloris viridis in Complex with NAD and PUT==		==Crystal Structure of the Homospermidine Synthase (HSS) variant W229A from Blastochloris viridis in Complex with NAD and PUT==
-	<StructureSection load='6s72' size='340' side='right'caption='[[6s72]]' scene=''>	+	<StructureSection load='6s72' size='340' side='right'caption='[[6s72]], [[Resolution\|resolution]] 1.87Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6S72 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6S72 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6s72]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Blastochloris_viridis Blastochloris viridis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6S72 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6S72 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=6s72 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6s72 OCA], [https://pdbe.org/6s72 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6s72 RCSB], [https://www.ebi.ac.uk/pdbsum/6s72 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6s72 ProSAT]</span></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]] 1.87Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=PUT:1,4-DIAMINOBUTANE'>PUT</scene></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=6s72 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6s72 OCA], [https://pdbe.org/6s72 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6s72 RCSB], [https://www.ebi.ac.uk/pdbsum/6s72 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6s72 ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/HSS_BLAVI HSS_BLAVI]
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Polyamines influence medically relevant processes in the opportunistic pathogen Pseudomonas aeruginosa, including virulence, biofilm formation and susceptibility to antibiotics. Although homospermidine synthase (HSS) is part of the polyamine metabolism in various strains of P. aeruginosa, neither its role nor its structure has been examined so far. The reaction mechanism of the nicotinamide adenine dinucleotide (NAD(+))-dependent bacterial HSS has previously been characterized based on crystal structures of Blastochloris viridis HSS (BvHSS). This study presents the crystal structure of P. aeruginosa HSS (PaHSS) in complex with its substrate putrescine. A high structural similarity between PaHSS and BvHSS with conservation of the catalytically relevant residues is demonstrated, qualifying BvHSS as a model for mechanistic studies of PaHSS. Following this strategy, crystal structures of single-residue variants of BvHSS are presented together with activity assays of PaHSS, BvHSS and BvHSS variants. For efficient homospermidine production, acidic residues are required at the entrance to the binding pocket (`ionic slide') and near the active site (`inner amino site') to attract and bind the substrate putrescine via salt bridges. The tryptophan residue at the active site stabilizes cationic reaction components by cation-pi interaction, as inferred from the interaction geometry between putrescine and the indole ring plane. Exchange of this tryptophan for other amino acids suggests a distinct catalytic requirement for an aromatic interaction partner with a highly negative electrostatic potential. These findings substantiate the structural and mechanistic knowledge on bacterial HSS, a potential target for antibiotic design.
		+
		+	Structural and catalytic characterization of Blastochloris viridis and Pseudomonas aeruginosa homospermidine synthases supports the essential role of cation-pi interaction.,Helfrich F, Scheidig AJ Acta Crystallogr D Struct Biol. 2021 Oct 1;77(Pt 10):1317-1335. doi:, 10.1107/S2059798321008937. Epub 2021 Sep 23. PMID:34605434<ref>PMID:34605434</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 6s72" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Blastochloris viridis]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Helfrich F]]		[[Category: Helfrich F]]
	[[Category: Scheidig AJ]]		[[Category: Scheidig AJ]]

OCA at 20:11, 20 October 2021

OCA — Wed, 20 Oct 2021 20:11:50 GMT

←Older revision		Revision as of 20:11, 20 October 2021
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-	'''Unreleased structure'''

-	~~The entry~~ 6s72 ~~is ON HOLD~~	+	==Crystal Structure of the Homospermidine Synthase (HSS) variant W229A from Blastochloris viridis in Complex with NAD and PUT==
-		+	<StructureSection load='6s72' size='340' side='right'caption='[[6s72]]' scene=''>
-	~~Authors~~:	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6S72 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6S72 FirstGlance]. <br>
-	~~Description~~:	+	</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=6s72 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6s72 OCA], [https://pdbe.org/6s72 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6s72 RCSB], [https://www.ebi.ac.uk/pdbsum/6s72 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6s72 ProSAT]</span></td></tr>
-	[[Category: ~~Unreleased~~ Structures]]	+	</table>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Helfrich F]]
		+	[[Category: Scheidig AJ]]

OCA: Protected "6s72" [edit=sysop:move=sysop]

OCA — Wed, 10 Jul 2019 04:29:37 GMT

Protected "6s72" [edit=sysop:move=sysop]

←Older revision

Revision as of 04:29, 10 July 2019

OCA: New page: '''Unreleased structure''' The entry 6s72 is ON HOLD Authors: Description: Category: Unreleased Structures

OCA — Wed, 10 Jul 2019 04:29:36 GMT

New page: '''Unreleased structure''' The entry 6s72 is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 6s72 is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]

6s72 - Revision history

OCA at 12:36, 24 January 2024

OCA at 20:11, 20 October 2021

OCA: Protected "6s72" [edit=sysop:move=sysop]

OCA: New page: '''Unreleased structure''' The entry 6s72 is ON HOLD Authors: Description: Category: Unreleased Structures