2B5Z

Hen lysozyme chemically glycosylated

Summary for 2B5Z

• Entry DOI: 10.2210/pdb2b5z/pdb
• Related: 132L 1IEE
• Descriptor: Lysozyme C, (1S)-1,5-anhydro-1-(ethylsulfonyl)-D-glucitol, AZIDE ION, ... (5 entities in total)
• Functional Keywords: chemical glycosylation, hydrolase
• Biological source: Gallus gallus (chicken)
• Cellular location: Secreted: P00698
• Total number of polymer chains: 1
• Total formula weight: 15574.41

Authors

Lopez-Jaramillo, F.J.,Perez-Balderas, F.,Hernandez-Mateo, F.,Santoyo-Gonzalez, F. (deposition date: 2005-09-29, release date: 2006-10-03, Last modification date: 2024-10-30)

Primary citation

Lopez-Jaramillo, F.J.,Perez-Banderas, F.,Hernandez-Mateo, F.,Santoyo-Gonzalez, F.
Production, crystallization and X-ray characterization of chemically glycosylated hen egg-white lysozyme.
Acta Crystallogr.,Sect.F, 61:435-438, 2005

PubMed Abstract: The crystallization of glycoproteins is one of the challenges to be confronted by the crystallographic community in the frame of what is known as glycobiology. The state of the art for the crystallization of glycoproteins is not promising and removal of the carbohydrate chains is generally suggested since they are flexible and a source of heterogeneity. In this paper, the feasibility of introducing glucose into the model protein hen egg-white lysozyme via a post-purification glycosylation reaction that may turn any protein into a model glycoprotein whose carbohydrate fraction can be manipulated is demonstrated.

PubMed: 16511062
DOI: 10.1107/S1744309105008869

Experimental method

X-RAY DIFFRACTION (1.6 Å)