1gd6 | pdb_00001gd6

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STRUCTURE OF THE BOMBYX MORI LYSOZYME

File:1gd6.gif


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1gd6, resolution 2.5Å
Activity: Lysozyme, with EC number 3.2.1.17
Coordinates: save as pdb, mmCIF, xml



Overview

Bombyx mori lysozyme (BmLZ), from the silkworm, is an insect lysozyme. BmLZ has considerable activity at low temperatures and low activation energies compared with those of hen egg white lysozyme (HEWLZ), according to measurements of the temperature dependencies of relative activity (lytic and glycol chitin) and the estimation of activation energies using the Arrhenius equation. Being so active at low temperatures and low activation energies is characteristic of psychrophilic (cold-adapted) enzymes. The three-dimensional structure of BmLZ has been determined by X-ray crystallography at 2.5 A resolution. The core structure of BmLZ is similar to that of c-type lysozymes. However, BmLZ shows some distinct differences in the two exposed loops and the C-terminal region. A detailed comparison of BmLZ and HEWLZ suggests structural rationalizations for the differences in the catalytic efficiency, stability, and mode of activity between these two lysozymes.

About this Structure

1GD6 is a Single protein structure of sequence from Bombyx mori. Full crystallographic information is available from OCA.

Reference

Structural analysis of an insect lysozyme exhibiting catalytic efficiency at low temperatures., Matsuura A, Yao M, Aizawa T, Koganesawa N, Masaki K, Miyazawa M, Demura M, Tanaka I, Kawano K, Nitta K, Biochemistry. 2002 Oct 8;41(40):12086-92. PMID:12356308

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