3w6a: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
No edit summary |
||
| (4 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==Crystal structure of cross-linked tetragonal hen egg white lysozyme soaked wiht 5mM [Ru(benzene)Cl2]2== | ==Crystal structure of cross-linked tetragonal hen egg white lysozyme soaked wiht 5mM [Ru(benzene)Cl2]2== | ||
<StructureSection load='3w6a' size='340' side='right' caption='[[3w6a]], [[Resolution|resolution]] 1.77Å' scene=''> | <StructureSection load='3w6a' size='340' side='right'caption='[[3w6a]], [[Resolution|resolution]] 1.77Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3w6a]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3w6a]] 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=3W6A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3W6A FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=RBN:BENZENERUTHENIUM(II)+CHLORIDE'>RBN</scene>, <scene name='pdbligand=RU:RUTHENIUM+ION'>RU</scene | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.77Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=RBN:BENZENERUTHENIUM(II)+CHLORIDE'>RBN</scene>, <scene name='pdbligand=RU:RUTHENIUM+ION'>RU</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=3w6a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w6a OCA], [https://pdbe.org/3w6a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3w6a RCSB], [https://www.ebi.ac.uk/pdbsum/3w6a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3w6a ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </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 == | |||
Porous protein crystals, which are protein assemblies in the solid state, have been engineered to form catalytic vessels by the incorporation of organometallic complexes. Ruthenium complexes in cross-linked porous hen egg white lysozyme (HEWL) crystals catalyzed the enantioselective hydrogen-transfer reduction of acetophenone derivatives. The crystals accelerated the catalytic reaction and gave different enantiomers based on the crystal form (tetragonal or orthorhombic). This method represents a new approach for the construction of bioinorganic catalysts from protein crystals. | |||
Porous protein crystals as catalytic vessels for organometallic complexes.,Tabe H, Abe S, Hikage T, Kitagawa S, Ueno T Chem Asian J. 2014 May;9(5):1373-8. doi: 10.1002/asia.201301347. Epub 2014 Feb , 13. PMID:24677803<ref>PMID:24677803</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3w6a" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Lysozyme 3D structures|Lysozyme 3D structures]] | *[[Lysozyme 3D structures|Lysozyme 3D structures]] | ||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Gallus gallus]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Abe | [[Category: Abe S]] | ||
[[Category: Hikage | [[Category: Hikage T]] | ||
[[Category: Kitagawa | [[Category: Kitagawa S]] | ||
[[Category: Tabe | [[Category: Tabe H]] | ||
[[Category: Ueno | [[Category: Ueno T]] | ||
Latest revision as of 05:35, 21 November 2024
Crystal structure of cross-linked tetragonal hen egg white lysozyme soaked wiht 5mM [Ru(benzene)Cl2]2Crystal structure of cross-linked tetragonal hen egg white lysozyme soaked wiht 5mM [Ru(benzene)Cl2]2
Structural highlights
FunctionLYSC_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 PubMedPorous protein crystals, which are protein assemblies in the solid state, have been engineered to form catalytic vessels by the incorporation of organometallic complexes. Ruthenium complexes in cross-linked porous hen egg white lysozyme (HEWL) crystals catalyzed the enantioselective hydrogen-transfer reduction of acetophenone derivatives. The crystals accelerated the catalytic reaction and gave different enantiomers based on the crystal form (tetragonal or orthorhombic). This method represents a new approach for the construction of bioinorganic catalysts from protein crystals. Porous protein crystals as catalytic vessels for organometallic complexes.,Tabe H, Abe S, Hikage T, Kitagawa S, Ueno T Chem Asian J. 2014 May;9(5):1373-8. doi: 10.1002/asia.201301347. Epub 2014 Feb , 13. PMID:24677803[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||