Structural highlights
4w96 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.
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| Method: | X-ray diffraction, Resolution 1.5Å |
| Ligands: | , , , , |
| 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.
See Also
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:http://dx.doi.org/10.1021/ic502159x
