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TitleHigh-resolution X-ray analysis reveals binding of arginine to aromatic residues of lysozyme surface: implication of suppression of protein aggregation by arginine
Journal, issue, pagesProtein Eng. Des. Sel., Vol. 24, Page 269-274, Year 2011
Publish dateMar 31, 2010 (structure data deposition date)
AuthorsIto, L. / Shiraki, K. / Matsuura, T. / Okumura, M. / Hasegawa, K. / Baba, S. / Yamaguchi, H. / Kumasaka, T.
External linksProtein Eng. Des. Sel. / PubMed:21084280
MethodsX-ray diffraction
Resolution1.2 - 1.6 Å
Structure data

PDB-3agg:
X-ray analysis of lysozyme in the absence of Arg
Method: X-RAY DIFFRACTION / Resolution: 1.6 Å

PDB-3agh:
X-ray analysis of lysozyme in the presence of 200 mM Arg
Method: X-RAY DIFFRACTION / Resolution: 1.49 Å

PDB-3agi:
High resolution X-ray analysis of Arg-lysozyme complex in the presence of 500 mM Arg
Method: X-RAY DIFFRACTION / Resolution: 1.2 Å

Chemicals

ChemComp-CL:
Unknown entry

ChemComp-NA:
Unknown entry

ChemComp-ACT:
ACETATE ION

ChemComp-HOH:
WATER

ChemComp-ARG:
ARGININE

Source
  • gallus gallus (chicken)
KeywordsHYDROLASE / lysozyme / glycosidase / arginine / Allergen / Antimicrobial / Bacteriolytic enzyme / Disulfide bond

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