2q0m

From Proteopedia

Tricarbonylmanganese(I)-lysozyme complex : a structurally characterized organometallic protein

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.
Method:	X-ray diffraction, Resolution 1.7Å
Ligands:	CL, CMO, MN, NA, TFS
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

Checkto colour the structure by Evolutionary Conservation, 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.

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Citations

8 reviews cite this structure

Modelling NiFe hydrogenases: nickel-based electrocatalysts for hydrogen production.

Canaguier et al. (2008)

7 more

11 other articles

No citations found

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

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

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PDB ID 2q0m

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2q0m

From Proteopedia

Tricarbonylmanganese(I)-lysozyme complex : a structurally characterized organometallic protein

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

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