1JEF

TURKEY LYSOZYME COMPLEX WITH (GLCNAC)3

Summary for 1JEF

• Entry DOI: 10.2210/pdb1jef/pdb
• Related PRD ID: PRD_900017
• Descriptor: LYSOZYME, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, SULFATE ION, ... (4 entities in total)
• Functional Keywords: enzyme, hydrolase, inhibitor complex, glycosidase, bacteriolytic enzyme
• Biological source: Meleagris gallopavo (turkey)
• Cellular location: Secreted: P00703
• Total number of polymer chains: 1
• Total formula weight: 14951.76

Authors

Harata, K.,Muraki, M. (deposition date: 1997-04-23, release date: 1997-10-15, Last modification date: 2024-10-16)

Primary citation

Harata, K.,Muraki, M.
X-ray structure of turkey-egg lysozyme complex with tri-N-acetylchitotriose. Lack of binding ability at subsite A.
Acta Crystallogr.,Sect.D, 53:650-657, 1997

PubMed Abstract: The turkey-egg lysozyme (TEL) complex with tri-N-acetylchitotriose [(GlcNac)3] was co-crystallized from 1.5% TEL and 2 mM (GlcNac)3 at pH 4.2. The crystal structure was determined by molecular replacement and refined to an R value of 0.182 using 10-1.77 A data. The (GlcNac)3 molecule occupies the subsites A, B and C. At the subsites B and C, the sugar residues are bound in a similar manner to that found in the hen-egg lysozyme (HEL) complex. In contrast, the GlcNac residue at the subsite A is exposed to bulk solvent and has no contact with the protein molecule because the active residue Asp101 in HEL is replaced by Gly in TEL. A sulfate ion is bound in the vicinity of subsite B and forms hydrogen bonds with the sugar residue and the guanidino group of Arg61, assisting the binding of the sugar residue to subsite B. The active-site cleft of TEL is narrower than that of native TEL, thus attaining the best fit of the (GlcNac)3 molecule. The lack of binding ability of subsite A is discussed in relation to the catalytic properties of TEL. The result suggests that the cleavage pattern of oligosaccharide substrates in the catalytic reaction is regulated by the protein-sugar interaction at subsite A.

PubMed: 15299852
DOI: 10.1107/S0907444997005362

Experimental method

X-RAY DIFFRACTION (1.77 Å)