Structural highlights
2q0m 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 1.7Å |
| 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]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The reaction of the new and structurally characterized covalent {Mn(CO)(3)(H(2)O)(2)}(+)-lysozyme adduct with NiS(4) and NiN(2)S(2) complexes generates binuclear Ni-Mn complexes; relevance to the reactivity of the protein-bound {Fe(CO)(CN)(2)} intermediate during maturation of [NiFe] hydrogenases is discussed.
Tricarbonylmanganese(I)-lysozyme complex: a structurally characterized organometallic protein.,Razavet M, Artero V, Cavazza C, Oudart Y, Lebrun C, Fontecilla-Camps JC, Fontecave M Chem Commun (Camb). 2007 Jul 19;(27):2805-7. Epub 2007 Jun 11. PMID:17609782[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
- ↑ Razavet M, Artero V, Cavazza C, Oudart Y, Lebrun C, Fontecilla-Camps JC, Fontecave M. Tricarbonylmanganese(I)-lysozyme complex: a structurally characterized organometallic protein. Chem Commun (Camb). 2007 Jul 19;(27):2805-7. Epub 2007 Jun 11. PMID:17609782 doi:http://dx.doi.org/10.1039/b703887a
