1BB7

LYSOZYME COMPLEX WITH 4-METHYL-UMBELLIFERYL CHITOBIOSE

Summary for 1BB7

• Entry DOI: 10.2210/pdb1bb7/pdb
• Descriptor: LYSOZYME, 4-METHYL-UMBELLIFERYL-N-ACETYL-CHITOBIOSE (3 entities in total)
• Functional Keywords: hydrolase, n-acetyl-muramidase, umbelliferone glycosides
• Biological source: Oncorhynchus mykiss (rainbow trout)
• Cellular location: Secreted: P11941
• Total number of polymer chains: 1
• Total formula weight: 14885.62

Authors

Vollan, V.B.,Hough, E.,Karlsen, S. (deposition date: 1998-04-29, release date: 1999-05-04, Last modification date: 2024-11-20)

Primary citation

Vollan, V.B.,Hough, E.,Karlsen, S.
Structural studies on the binding of 4-methylumbelliferone glycosides of chitin to rainbow trout lysozyme.
Acta Crystallogr.,Sect.D, 55:60-66, 1999

PubMed Abstract: Two complexes between rainbow trout lysozyme (RBTL) and 4-methylumbelliferyl chitobioside, 4MeU-(GlcNAc)2, and chitotrioside, 4MeU-(GlcNAc)3, were produced by co-crystallization and soaking, respectively, and the crystal structures were solved at 2.0 A resolution. The results show that 4-MeU-(GlcNAc)3 binds in subsites A-D and that 4-MeU-(GlcNAc)2 binds in subsites B-D in the active-site cleft of RBTL. This agrees well with earlier crystallographic studies on the binding of oligosaccharides of chitin to RBTL, which showed that (GlcNAc)3 binds to sites B-D in RBTL and not to A-C as seen in the human and turkey egg-white lysozymes. For both complexes the 4-MeU moiety in site D has diffuse electron density and is flexible, as it is only bound to water molecules and not to the protein. Since no electron density was observed in site E, the solved structures give views of nonproductive enzyme-substrate complexes.

PubMed: 10089395
DOI: 10.1107/S0907444998006623

Experimental method

X-RAY DIFFRACTION (2 Å)