PDBsum entry 1ja2

Hydrolase

PDB id: 1ja2

Contents

Protein chain

129 a.a. *

* Residue conservation analysis

PDB id:

1ja2

Name:

Hydrolase

Title:

Binding of n-acetylglucosamine to chicken egg lysozyme: a powder diffraction study

Structure:

Lysozyme. Chain: a. Synonym: 1,4-beta-n-acetylmuramidasE C. Allergen gal d 4. Gal d iv. Engineered: yes

Source:

Gallus gallus. Chicken. Organism_taxid: 9031. Cellular_location: cytoplasm. Expressed in: escherichia coli. Expression_system_taxid: 562

Biol. unit:

Dimer (from PQS)

Authors:

R.B.Von Dreele

Key ref:

R.B.Von Dreele (2001). Binding of N-acetylglucosamine to chicken egg lysozyme: a powder diffraction study. Acta Crystallogr D Biol Crystallogr, 57, 1836-1842. PubMed id: 11717496 DOI: 10.1107/S0907444901015748

Date:

29-May-01 Release date: 15-Jun-01

Protein chain

P00698  (LYSC_CHICK) -  Lysozyme C from Gallus gallus

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.

DOI no: 10.1107/S0907444901015748

Acta Crystallogr D Biol Crystallogr 57:1836-1842 (2001)

PubMed id: 11717496

Binding of N-acetylglucosamine to chicken egg lysozyme: a powder diffraction study.

R.B.Von Dreele.

ABSTRACT

The binding of N-acetylglucosamine (NAG) to chicken egg lysozyme (E.C. 3.2.1.17) was investigated by high-resolution X-ray powder diffraction at room temperature. NAG was found to bind to lysozyme in a rapid precipitation preparation with 0.05 M NaCl buffer pH 6.0, but not 0.05 M NaCl buffer pH 5.0. Binding was indicated by significant and readily apparent changes in the diffraction pattern from that of the apo protein precipitated from the same solvent. The location of NAG bound to lysozyme was easily found from a difference Fourier map generated from structure factors extracted during a preliminary combined Rietveld and stereochemical restraint refinement. Full protein and protein-NAG structures were refined with these techniques (R(wp) = 2.22-2.49%, R(p) = 1.79-1.95%, R(F)(2) = 4.95-6.35%) and revealed a binding mode for NAG which differed from that found in an earlier single-crystal study and probably represents a precursor trapped by rapid precipitation.

Selected figure(s)

Figure 3.
Figure 3 Stereographic representation of the F map at 1.5 . The map was developed from structure factors extracted during the Rietveld refinement of the lysozyme structure using the diffraction data obtained from the 0.5 M NaCl pH 6.0 NAG-lysozyme material. Superimposed are the NAG molecule (shown in red) found by the final Rietveld refinement of the NAG-lysozyme complex and the NAG molecule (shown in green) found by the single-crystal analysis of Perkins et al. (1978[Perkins, S. J., Johnson, L. N., Machin, P. A. & Phillips, D. C. (1978). Biochem. J. 173, 607-616.]).

Figure 6.
Figure 6 Steroscopic view of molecular surface of lysozyme with a CPK representation of the bound N-acetylglucosamine. The protein surface is colored according to the electrostatic potential, where blue is positive and red negative.

The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2001, 57, 1836-1842) copyright 2001.

Figures were selected by an automated process.