8bpj - Revision history

OCA at 08:19, 7 February 2024

2024-02-07T08:19:25Z

←Older revision		Revision as of 08:19, 7 February 2024
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	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/LYSC_CHICK LYSC_CHICK] Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Has bacteriolytic activity against M.luteus.<ref>PMID:22044478</ref>		[https://www.uniprot.org/uniprot/LYSC_CHICK LYSC_CHICK] Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Has bacteriolytic activity against M.luteus.<ref>PMID:22044478</ref>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The paddlewheel [Ru(2)Cl(O(2)CCH(3))(4)] complex was previously reported to react with the model protein hen egg white lysozyme (HEWL), forming adducts with two diruthenium moieties bound to Asp101 and Asp119 side chains upon the release of one acetate. To study the effect of the equatorial ligands on the reactivity with proteins of diruthenium compounds, X-ray structures of the adducts formed when HEWL reacts with [Ru(2)Cl(D-p-FPhF)(O(2)CCH(3))(3)] [D-p-FPhF = N,N'-bis(4-fluorophenyl)formamidinate] under different conditions were solved. [Ru(2)Cl(D-p-FPhF)(O(2)CCH(3))(3)] is bonded through their equatorial positions to the Asp side chains. Protein binding occurs cis or trans to D-p-FPhF. Lys or Arg side chains or even main-chain carbonyl groups can coordinate to the diruthenium core at the axial site. Data help to understand the reactivity of paddlewheel diruthenium complexes with proteins, providing useful information for the design of new artificial diruthenium-containing metalloenzymes with potential applications in the fields of catalysis, biomedicine, and biotechnology.
-
-	Effect of Equatorial Ligand Substitution on the Reactivity with Proteins of Paddlewheel Diruthenium Complexes: Structural Studies.,Teran A, Ferraro G, Sanchez-Pelaez AE, Herrero S, Merlino A Inorg Chem. 2023 Jan 16;62(2):670-674. doi: 10.1021/acs.inorgchem.2c04103. Epub , 2023 Jan 4. PMID:36597851<ref>PMID:36597851</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 8bpj" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 21:14, 28 June 2023

2023-06-28T21:14:48Z

←Older revision		Revision as of 21:14, 28 June 2023
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 8bpj is ~~ON HOLD until Paper~~ Publication	+	==X-ray structure of the adduct formed upon reaction of Lysozyme with [Ru2Cl(D-p-FPhF)(O2CCH3)3] (Structure 1)==
		+	<StructureSection load='8bpj' size='340' side='right'caption='[[8bpj]], [[Resolution\|resolution]] 1.38Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[8bpj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8BPJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8BPJ FirstGlance]. <br>
		+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 1.38Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene>, <scene name='pdbligand=TZ6:9,11-bis(4-fluorophenyl)-3,7-dimethyl-2,4,6,8-tetraoxa-9,11-diaza-1$l^{4},5$l^{4}-diruthenatricyclo[3.3.3.0^{1,5}]undecane'>TZ6</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=8bpj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8bpj OCA], [https://pdbe.org/8bpj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8bpj RCSB], [https://www.ebi.ac.uk/pdbsum/8bpj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8bpj ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/LYSC_CHICK LYSC_CHICK] Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Has bacteriolytic activity against M.luteus.<ref>PMID:22044478</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The paddlewheel [Ru(2)Cl(O(2)CCH(3))(4)] complex was previously reported to react with the model protein hen egg white lysozyme (HEWL), forming adducts with two diruthenium moieties bound to Asp101 and Asp119 side chains upon the release of one acetate. To study the effect of the equatorial ligands on the reactivity with proteins of diruthenium compounds, X-ray structures of the adducts formed when HEWL reacts with [Ru(2)Cl(D-p-FPhF)(O(2)CCH(3))(3)] [D-p-FPhF = N,N'-bis(4-fluorophenyl)formamidinate] under different conditions were solved. [Ru(2)Cl(D-p-FPhF)(O(2)CCH(3))(3)] is bonded through their equatorial positions to the Asp side chains. Protein binding occurs cis or trans to D-p-FPhF. Lys or Arg side chains or even main-chain carbonyl groups can coordinate to the diruthenium core at the axial site. Data help to understand the reactivity of paddlewheel diruthenium complexes with proteins, providing useful information for the design of new artificial diruthenium-containing metalloenzymes with potential applications in the fields of catalysis, biomedicine, and biotechnology.

-	~~Authors~~: ~~Teran~~, A., ~~Merlino~~, A., ~~Ferraro, G~~.	+	Effect of Equatorial Ligand Substitution on the Reactivity with Proteins of Paddlewheel Diruthenium Complexes: Structural Studies.,Teran A, Ferraro G, Sanchez-Pelaez AE, Herrero S, Merlino A Inorg Chem. 2023 Jan 16;62(2):670-674. doi: 10.1021/acs.inorgchem.2c04103. Epub , 2023 Jan 4. PMID:36597851<ref>PMID:36597851</ref>

-	~~Description: X-ray structure~~ of the ~~adduct formed upon reaction~~ of ~~Lysozyme with [Ru2Cl(D~~-p-~~FPhF)(O2CCH3)3] (Structure 1)~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased Structures~~]]	+	</div>
-	[[Category: ~~Teran, A~~]]	+	<div class="pdbe-citations 8bpj" style="background-color:#fffaf0;"></div>
-	[[Category: Ferraro, G]]	+	== References ==
-	[[Category: Merlino, A]]	+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Gallus gallus]]
		+	[[Category: Large Structures]]
		+	[[Category: Ferraro G]]
		+	[[Category: Merlino A]]
		+	[[Category: Teran A]]

OCA at 09:17, 22 February 2023

2023-02-22T09:17:29Z

←Older revision		Revision as of 09:17, 22 February 2023
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	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 8bpj is ON HOLD	+	The entry 8bpj is ON HOLD until Paper Publication

	Authors: Teran, A., Merlino, A., Ferraro, G.		Authors: Teran, A., Merlino, A., Ferraro, G.

OCA: Protected "8bpj" [edit=sysop:move=sysop]

2023-01-25T04:48:07Z

Protected "8bpj" [edit=sysop:move=sysop]

←Older revision

Revision as of 04:48, 25 January 2023

OCA: New page: '''Unreleased structure''' The entry 8bpj is ON HOLD Authors: Teran, A., Merlino, A., Ferraro, G. Description: X-ray structure of the adduct formed upon reaction of Lysozyme with [Ru2C...

2023-01-25T04:48:06Z

New page: '''Unreleased structure''' The entry 8bpj is ON HOLD Authors: Teran, A., Merlino, A., Ferraro, G. Description: X-ray structure of the adduct formed upon reaction of Lysozyme with [Ru2C...

New page

'''Unreleased structure'''

The entry 8bpj is ON HOLD

Authors: Teran, A., Merlino, A., Ferraro, G.

Description: X-ray structure of the adduct formed upon reaction of Lysozyme with [Ru2Cl(D-p-FPhF)(O2CCH3)3] (Structure 1)
[[Category: Unreleased Structures]]
[[Category: Teran, A]]
[[Category: Ferraro, G]]
[[Category: Merlino, A]]