3AJN

Structural basis of glycine amide on suppression of protein aggregation by high resolution X-ray analysis

Replaces:  2ZXS

Summary for 3AJN

• Entry DOI: 10.2210/pdb3ajn/pdb
• Descriptor: Lysozyme C, AMINOMETHYLAMIDE, CHLORIDE ION, ... (5 entities in total)
• Functional Keywords: hydrolase, lysozyme, glycosidase, glycine amide
• Biological source: Gallus gallus (Chicken)
• Cellular location: Secreted: P00698
• Total number of polymer chains: 1
• Total formula weight: 14721.38

Authors

Ito, L.,Shiraki, K.,Hasegawa, K.,Kumasaka, T. (deposition date: 2010-06-09, release date: 2011-02-16, Last modification date: 2024-10-23)

Primary citation

Ito, L.,Shiraki, K.,Makino, M.,Hasegawa, K.,Kumasaka, T.
Glycine amide shielding on the aromatic surfaces of lysozyme: Implication for suppression of protein aggregation
Febs Lett., 585:555-560, 2011

PubMed Abstract: Glycine amide (GlyAd), a typically amidated amino acid, is a versatile additive that suppresses protein aggregation during refolding, heat treatment, and crystallization. In spite of its effectiveness, the exact mechanism by which GlyAd suppresses protein aggregation remains to be elucidated. Here, we show the crystal structure of the GlyAd-lysozyme complex by high resolution X-ray crystallographic analysis at a 1.05Å resolution. GlyAd bound to the lysozyme surface near aromatic residues and decreased the amount of bound waters and increased the mobility of protein. Arg and GlyAd molecules are different in binding sites and patterns from glycerol and related compounds, indicating that decreasing hydrophobic patches might be involved in suppression of protein aggregation.

PubMed: 21237160
DOI: 10.1016/j.febslet.2011.01.008

Experimental method

X-RAY DIFFRACTION (1.05 Å)