3AGH

X-ray analysis of lysozyme in the presence of 200 mM Arg

Summary for 3AGH

• Entry DOI: 10.2210/pdb3agh/pdb
• Related: 3A34 3AGG 3AGI
• Descriptor: Lysozyme C, ACETATE ION, SODIUM ION, ... (5 entities in total)
• Functional Keywords: hydrolase, lysozyme, glycosidase, arginine, allergen, antimicrobial, bacteriolytic enzyme, disulfide bond
• Biological source: Gallus gallus (chicken)
• Cellular location: Secreted: P00698
• Total number of polymer chains: 1
• Total formula weight: 14555.01

Authors

Ito, L.,Shiraki, K.,Hasegawa, K.,Baba, S.,Kumasaka, T. (deposition date: 2010-03-31, release date: 2011-03-23, Last modification date: 2024-10-30)

Primary citation

Ito, L.,Shiraki, K.,Matsuura, T.,Okumura, M.,Hasegawa, K.,Baba, S.,Yamaguchi, H.,Kumasaka, T.
High-resolution X-ray analysis reveals binding of arginine to aromatic residues of lysozyme surface: implication of suppression of protein aggregation by arginine
Protein Eng.Des.Sel., 24:269-274, 2011

PubMed Abstract: While biotechnological applications of arginine (Arg) as a solution additive that prevents protein aggregation are increasing, the molecular mechanism of its effects remains unclear. In this study, we investigated the Arg-lysozyme complex by high-resolution crystallographic analysis. Three Arg molecules were observed to be in close proximity to aromatic amino acid residues of the protein surface, and their occupancies gradually increased with increasing Arg concentration. These interactions were mediated by electrostatic, hydrophobic and cation-π interactions with the surface residues. The binding of Arg decreased the accessible surface area of aromatic residues by 40%, but increased that of charged residues by 10%. These changes might prevent intermolecular hydrophobic interactions by shielding hydrophobic regions of the lysozyme surface, resulting in an increase in protein solubility.

PubMed: 21084280
DOI: 10.1093/protein/gzq101

Experimental method

X-RAY DIFFRACTION (1.49 Å)