2aub

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Lysozyme structure derived from thin-film-based crystals

Structural highlights

2aub 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
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 present report is dedicated to a systematic comparison of crystal structures produced by the nanobiofilm template method and by the classical hanging-drop vapour-diffusion method. Crystals grown by the innovative nanostructured template method appear indeed radiation-resistant even in the presence of a third-generation highly focused beam at the European Synchrotron Radiation Facility. The implications of this finding for protein crystallography are discussed here in terms of water redistribution and of the detailed atomic resolution comparative studies of the two crystal structures with or without nanobiofilm template, as emerging also from circular-dichroism and thermal denaturation studies.

Comparison of lysozyme structures derived from thin-film-based and classical crystals.,Pechkova E, Sivozhelezov V, Tropiano G, Fiordoro S, Nicolini C Acta Crystallogr D Biol Crystallogr. 2005 Jun;61(Pt 6):803-8. Epub 2005, May 26. PMID:15930644[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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Citations
0 reviews cite this structure
Protein thermal stability: the role of protein structure and aqueous environment.
Pechkova et al. (2007)
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2 other articles
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See Also

References

  1. ↑ 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
  2. ↑ Pechkova E, Sivozhelezov V, Tropiano G, Fiordoro S, Nicolini C. Comparison of lysozyme structures derived from thin-film-based and classical crystals. Acta Crystallogr D Biol Crystallogr. 2005 Jun;61(Pt 6):803-8. Epub 2005, May 26. PMID:15930644 doi:10.1107/S0907444905006578

Contents


PDB ID 2aub

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