LYSOZYME GROWN AT BASIC PH AND ITS LOW HUMIDITY VARIANTLYSOZYME GROWN AT BASIC PH AND ITS LOW HUMIDITY VARIANT

Structural highlights

1hsx 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 1.9Å
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 structures of orthorhombic lysozyme grown at basic pH and its low-humidity variant have been solved and refined at 1.9 and 2.0 A resolution, respectively. A comparison of the native structure with those of crystals grown at acidic pH does not show any systematic pH-dependent difference in the molecular geometry. The conformations, mutual orientation and interactions of the catalytic residues Glu35 and Asp52 also remain unchanged. However, comparison between the native and low-humidity forms in the orthorhombic form show that the changes in molecular geometry which accompany the water-mediated transformation to the low-humidity form are more pronounced in the C-terminal residues than in the other regions of the molecule. During the transformation from the native to the low-humidity form, the locations of only about half the water molecules in the hydration shell remain unchanged, but the hydration shell as a whole moves along with the protein molecule.

Structures of orthorhombic lysozyme grown at basic pH and its low-humidity variant.,Sukumar N, Biswal BK, Vijayan M Acta Crystallogr D Biol Crystallogr. 1999 Apr;55(Pt 4):934-7. PMID:10089340[2]

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

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. Sukumar N, Biswal BK, Vijayan M. Structures of orthorhombic lysozyme grown at basic pH and its low-humidity variant. Acta Crystallogr D Biol Crystallogr. 1999 Apr;55(Pt 4):934-7. PMID:10089340

1hsx, resolution 1.90Å

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