2xjw: Difference between revisions
No edit summary |
No edit summary |
||
Line 8: | Line 8: | ||
<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=2xjw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xjw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xjw RCSB], [http://www.ebi.ac.uk/pdbsum/2xjw PDBsum]</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=2xjw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xjw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xjw RCSB], [http://www.ebi.ac.uk/pdbsum/2xjw PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[http://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;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Line 25: | Line 27: | ||
[[Category: Gallus gallus]] | [[Category: Gallus gallus]] | ||
[[Category: Lysozyme]] | [[Category: Lysozyme]] | ||
[[Category: Mukhopadkyay, A | [[Category: Mukhopadkyay, A]] | ||
[[Category: Romao, M J | [[Category: Romao, M J]] | ||
[[Category: Santos-Silva, T | [[Category: Santos-Silva, T]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Metal-protein adduct]] | [[Category: Metal-protein adduct]] |
Revision as of 11:07, 25 December 2014
LYSOZYME-CO RELEASING MOLECULE ADDUCTLYSOZYME-CO RELEASING MOLECULE ADDUCT
Structural highlightsFunction[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 PubMedCORM-3, [fac-Ru(CO)(3)Cl(kappa(2)-H(2)NCH(2)CO(2))], is a well-known carbon monoxide releasing molecule (CORM) capable of delivering CO in vivo. Herein we show for the first time that the interactions of CORM-3 with proteins result in the loss of a chloride ion, glycinate, and one CO ligand. The rapid formation of stable adducts between the protein and the remaining cis-Ru(II)(CO)(2) fragments was confirmed by Inductively Coupled Plasma-Atomic Emission Spectrocopy (ICP-AES), Liquid-Chromatography Mass Spectrometry (LC-MS), Infrared Spectroscopy (IR), and X-ray crystallography. Three Ru coordination sites are observed in the structure of hen egg white lysozyme crystals soaked with CORM-3. The site with highest Ru occupancy (80%) shows a fac-[(His15)Ru(CO)(2)(H(2)O)(3)] structure. CORM-3 Reactivity toward Proteins: The Crystal Structure of a Ru(II) Dicarbonyl-Lysozyme Complex.,Santos-Silva T, Mukhopadhyay A, Seixas JD, Bernardes GJ, Romao CC, Romao MJ J Am Chem Soc. 2011 Jan 4. PMID:21204537[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
|