PDBsum entry 1lyd

Hydrolase (o-glycosyl)

PDB id: 1lyd

Contents

Protein chain

164 a.a. *

Waters ×82

* Residue conservation analysis

PDB id:

1lyd

Name:

Hydrolase (o-glycosyl)

Title:

Crystal structure of t4-lysozyme generated from synthetic coding DNA expressed in escherichia coli

Structure:

T4 lysozyme. Chain: a. Engineered: yes

Source:

Enterobacteria phage t4. Organism_taxid: 10665

Biol. unit:

Dimer (from PQS)

Resolution:

2.00Å R-factor: 0.191

Authors:

D.R.Rose

Key ref:

D.R.Rose et al. (1988). Crystal structure of T4-lysozyme generated from synthetic coding DNA expressed in Escherichia coli. Protein Eng, 2, 277-282. PubMed id: 3074306

Date:

11-Jan-89 Release date: 15-Apr-90

Protein chain

P00720  (ENLYS_BPT4) -  Endolysin from Enterobacteria phage T4

Seq: 164 a.a.

Struc: 164 a.a.*

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

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.

Protein Eng 2:277-282 (1988)

PubMed id: 3074306

Crystal structure of T4-lysozyme generated from synthetic coding DNA expressed in Escherichia coli.

D.R.Rose, J.Phipps, J.Michniewicz, G.I.Birnbaum, F.R.Ahmed, A.Muir, W.F.Anderson, S.Narang.

ABSTRACT

The polypeptide produced by expressing a chemically synthesized gene coding for the amino-acid sequence of T4-lysozyme has been crystallized and subjected to X-ray diffraction. The crystal structure has been refined to a standard R-factor of 0.191 for data between 8 and 2 A resolution. The refined model is essentially the same as the well-known structure of wild-type T4-lysozyme determined previously by Matthews et al. (1987). Some small changes in the C-terminal region, which is important in maintaining the folded structure, have been noted. In addition to confirming that the synthetic gene product is very close to the wild type, this structure provides a benchmark for protein engineering experiments on the folding and the catalytic activity of this molecule by the method of gene synthesis.