1LZY

X-RAY STRUCTURE OF TURKEY EGG LYSOZYME COMPLEX WITH DI-N-ACETYLCHITOBIOSE. RECOGNITION AND BINDING OF ALPHA-ANOMERIC FORM

Summary for 1LZY

• Entry DOI: 10.2210/pdb1lzy/pdb
• Descriptor: TURKEY EGG WHITE LYSOZYME, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-alpha-D-glucopyranose (3 entities in total)
• Functional Keywords: hydrolase (o-glycosyl)
• Biological source: Meleagris gallopavo (turkey)
• Cellular location: Secreted: P00703
• Total number of polymer chains: 1
• Total formula weight: 14652.51

Authors

Harata, K. (deposition date: 1995-01-09, release date: 1995-02-27, Last modification date: 2024-10-23)

Primary citation

Harata, K.
X-ray structure of monoclinic turkey egg lysozyme at 1.3 A resolution.
Acta Crystallogr.,Sect.D, 49:497-504, 1993

PubMed Abstract: Monoclinic crystals of turkey egg lysozyme (TEL, E.C. 3.2.1.17) were obtained from 2.2 M ammonium sulfate solution at pH 4.2. They belong to space group P2(1) with unit-cell dimensions a = 38.07, b = 33.20, c = 46.12 A and beta = 110.1 degrees, and contain one molecule in the asymmetric unit (V(m) = 1.91 A(3) Da(-1)). The three-dimensional structure of TEL was solved by the method of multiple isomorphous replacement with anomalous scattering. Area detector data to 1.5 A resolution from native and heavy-atom derivatives were used for the structure determination. The structure was refined by the simulated-annealing method with diffraction data of 10-1.30 A resolution. The conventional R factor was 0.189. The root-mean-square deviations from ideal bond distances and angles were 0.016 A and 2.9 degrees, respectively. The backbone structure of TEL is very similar to that of hen egg lysozyme (HEL) and the difference in seven amino-acid residues does not affect the basic folding of the polypeptide chain. Except for the region from Gly101 to Gly104, the geometry of the active-site cleft is conserved between TEL and HEL. The Gly101 residue is located at the end of the sugar-binding site and the structural change in this region between TEL and HEL is considered to be responsible for the difference in their enzymatic properties.

PubMed: 15299509
DOI: 10.1107/S0907444993005542

Experimental method

X-RAY DIFFRACTION (1.55 Å)