PDBsum entry: 135l

Hydrolase(o-glycosyl)

PDB id: 135l

Contents

Protein chain

129 a.a. *

Waters ×114

* Residue conservation analysis

PDB id:

135l

Name:

Hydrolase(o-glycosyl)

Title:

X-ray structure of monoclinic turkey egg lysozyme at 1.3 angstroms resolution

Structure:

Turkey egg white lysozyme. Chain: a. Engineered: yes

Source:

Meleagris gallopavo. Turkey. Organism_taxid: 9103. Tissue: egg white

Resolution:

1.30Å R-factor: 0.189

Authors:

K.Harata

Key ref:

K.Harata (1993). X-ray structure of monoclinic turkey egg lysozyme at 1.3 A resolution. Acta Crystallogr D Biol Crystallogr, 49, 497-504. PubMed id: 15299509 DOI: 10.1107/S0907444993005542

Date:

10-Jun-93 Release date: 31-Oct-93

Supersedes:

1lz3

Protein chain

P00703  (LYSC_MELGA) -  Lysozyme C

Seq: 147 a.a.

Struc: 129 a.a.

Enzyme reactions

• Enzyme class: E.C.3.2.1.17 - Lysozyme.
• Reaction: Hydrolysis of the 1,4-beta-linkages between N-acetyl-D-glucosamine and N-acetylmuramic acid in peptidoglycan heteropolymers of the prokaryotes cell walls.

 Gene Ontology (GO) functional annotation 

• Cellular component: extracellular region (1 term)
• Biological process: metabolic process (4 terms)
• Biochemical function: catalytic activity (4 terms)

DOI no: 10.1107/S0907444993005542

Acta Crystallogr D Biol Crystallogr 49:497-504 (1993)

PubMed id: 15299509

X-ray structure of monoclinic turkey egg lysozyme at 1.3 A resolution.

K.Harata.

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.

Selected figure(s)

Figure 7.
Fig. 7. Structure of the active-site region. Water molecules are shown by shaded circles. Inter- molecular distances less than 3.2 A, involving side-chain atoms and water molecules, are shown by thin lines. Subsites for the binding of sugar residues arc denoted A--E.

Figure 8.
Fig. 8. Hydrogen-bond network in the active-site cleft. Distances less than 3.3 A are denoted by dashed lines. Water molecules are shown by full circles.

The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (1993, 49, 497-504) copyright 1993.

Figures were selected by an automated process.