4w94: Difference between revisions

Latest revision as of 15:21, 8 November 2023

Crystal structure of cross-linked tetragonal hen egg white lysozyme soaked with 5mM [Ru(CO)3Cl2]2

Structural highlights

4w94 is a 1 chain structure with sequence from Gallus gallus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.55Å
Ligands:	CL, DMF, NA, RU, RU1
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.^[1]

Publication Abstract from PubMed

Protein crystals generally are stable solid protein assemblies. Certain protein crystals are suitable for use as nanovessels for immobilizing metal complexes. Here we report the preparation of ruthenium carbonyl-incorporated cross-linked hen egg white lysozyme crystals (Ru.CL-HEWL). Ru.CL-HEWL retains a Ru carbonyl moiety that can release CO, although a composite of Ru carbonyl-HEWL dissolved in buffer solution (Ru.HEWL) does not release CO. We found that treatment of cells with Ru.CL-HEWL significantly increased nuclear factor kappa B (NF-kappaB) activity as a cellular response to CO. These results demonstrate that Ru.CL-HEWL has potential for use as an artificial extracellular scaffold suitable for transport and release of a gas molecule.

Preparation of a Cross-Linked Porous Protein Crystal Containing Ru Carbonyl Complexes as a CO-Releasing Extracellular Scaffold.,Tabe H, Fujita K, Abe S, Tsujimoto M, Kuchimaru T, Kizaka-Kondoh S, Takano M, Kitagawa S, Ueno T Inorg Chem. 2014 Dec 15. PMID:25494847^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Maehashi K, Matano M, Irisawa T, Uchino M, Kashiwagi Y, Watanabe T. Molecular characterization of goose- and chicken-type lysozymes in emu (Dromaius novaehollandiae): evidence for extremely low lysozyme levels in emu egg white. Gene. 2012 Jan 15;492(1):244-9. doi: 10.1016/j.gene.2011.10.021. Epub 2011 Oct, 25. PMID:22044478 doi:10.1016/j.gene.2011.10.021
↑ Tabe H, Fujita K, Abe S, Tsujimoto M, Kuchimaru T, Kizaka-Kondoh S, Takano M, Kitagawa S, Ueno T. Preparation of a Cross-Linked Porous Protein Crystal Containing Ru Carbonyl Complexes as a CO-Releasing Extracellular Scaffold. Inorg Chem. 2014 Dec 15. PMID:25494847 doi:https://dx.doi.org/10.1021/ic502159x

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Maehashi K, Matano M, Irisawa T, Uchino M, Kashiwagi Y, Watanabe T. Molecular characterization of goose- and chicken-type lysozymes in emu (Dromaius novaehollandiae): evidence for extremely low lysozyme levels in emu egg white. Gene. 2012 Jan 15;492(1):244-9. doi: 10.1016/j.gene.2011.10.021. Epub 2011 Oct, 25. PMID:22044478 doi:10.1016/j.gene.2011.10.021

[2] Tabe H, Fujita K, Abe S, Tsujimoto M, Kuchimaru T, Kizaka-Kondoh S, Takano M, Kitagawa S, Ueno T. Preparation of a Cross-Linked Porous Protein Crystal Containing Ru Carbonyl Complexes as a CO-Releasing Extracellular Scaffold. Inorg Chem. 2014 Dec 15. PMID:25494847 doi:https://dx.doi.org/10.1021/ic502159x

[1]

[2]

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 4w94 is ON HOLD
+==Crystal structure of cross-linked tetragonal hen egg white lysozyme soaked with 5mM [Ru(CO)3Cl2]2==
+<StructureSection load='4w94' size='340' side='right'caption='[[4w94]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4w94]] 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=4W94 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4W94 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]] 1.55&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DMF:DIMETHYLFORMAMIDE'>DMF</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=RU:RUTHENIUM+ION'>RU</scene>, <scene name='pdbligand=RU1:BIS(OXIDANIUMYLIDYNEMETHYL)RUTHENIUM(2+)'>RU1</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=4w94 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4w94 OCA], [https://pdbe.org/4w94 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4w94 RCSB], [https://www.ebi.ac.uk/pdbsum/4w94 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4w94 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 ==
+Protein crystals generally are stable solid protein assemblies. Certain protein crystals are suitable for use as nanovessels for immobilizing metal complexes. Here we report the preparation of ruthenium carbonyl-incorporated cross-linked hen egg white lysozyme crystals (Ru.CL-HEWL). Ru.CL-HEWL retains a Ru carbonyl moiety that can release CO, although a composite of Ru carbonyl-HEWL dissolved in buffer solution (Ru.HEWL) does not release CO. We found that treatment of cells with Ru.CL-HEWL significantly increased nuclear factor kappa B (NF-kappaB) activity as a cellular response to CO. These results demonstrate that Ru.CL-HEWL has potential for use as an artificial extracellular scaffold suitable for transport and release of a gas molecule.
-Authors: Tabe, H., Fujita, K., Abe, S., Tsujimoto, M., Kuchimaru, T., Kizaka-Kondo, S., Takano, M., Kitagawa, S., Ueno, T.
+Preparation of a Cross-Linked Porous Protein Crystal Containing Ru Carbonyl Complexes as a CO-Releasing Extracellular Scaffold.,Tabe H, Fujita K, Abe S, Tsujimoto M, Kuchimaru T, Kizaka-Kondoh S, Takano M, Kitagawa S, Ueno T Inorg Chem. 2014 Dec 15. PMID:25494847<ref>PMID:25494847</ref>
-Description: Crystal structure of cross-linked tetragonal hen egg white lysozyme soaked with 5mM [Ru(CO)3Cl2]2
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Fujita, K]]
+<div class="pdbe-citations 4w94" style="background-color:#fffaf0;"></div>
-[[Category: Kizaka-Kondo, S]]
-[[Category: Tsujimoto, M]]
+==See Also==
-[[Category: Kitagawa, S]]
+*[[Lysozyme 3D structures|Lysozyme 3D structures]]
-[[Category: Takano, M]]
+== References ==
-[[Category: Abe, S]]
+<references/>
-[[Category: Ueno, T]]
+__TOC__
-[[Category: Kuchimaru, T]]
+</StructureSection>
-[[Category: Tabe, H]]
+[[Category: Gallus gallus]]
+[[Category: Large Structures]]
+[[Category: Abe S]]
+[[Category: Fujita K]]
+[[Category: Kitagawa S]]
+[[Category: Kizaka-Kondo S]]
+[[Category: Kuchimaru T]]
+[[Category: Tabe H]]
+[[Category: Takano M]]
+[[Category: Tsujimoto M]]
+[[Category: Ueno T]]

4w94: Difference between revisions

Latest revision as of 15:21, 8 November 2023

Crystal structure of cross-linked tetragonal hen egg white lysozyme soaked with 5mM [Ru(CO)3Cl2]2

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools