Crystallization and preliminary X‐ray crystallographic studies of UDP‐N‐acetylenolpyruvylglucosamine reductase
Open Access
- 1 July 1994
- journal article
- for the-record
- Published by Wiley in Protein Science
- Vol. 3 (7) , 1125-1127
- https://doi.org/10.1002/pro.5560030718
Abstract
The overexpression and purification of the second enzyme in Escherichia coli peptidoglycan biosynthesis, UDP‐N‐acetylenolpyruvylglucosamine reductase (MurB), provided sufficient protein to undertake crystallization and X‐ray crystallographic studies of the enzyme. MurB crystallizes in 14–20% PEG 8000, 100 mM sodium cacodylate, pH 8.0, and 200 mM calcium acetate in the presence of its substrate UDP‐N‐acetylglucosamine enolpyruvate. Crystals of MurB belong to the tetragonal space group P41212 with a = b = 49.6 Å, c = 263.2 Å, and α = β = γ = 90° at –160 °C and diffract to at least 2.5 Å. Screening for heavy atom derivatives has yielded a single site that is reactive with both methylmercury nitrate and Thimerosal.Keywords
This publication has 6 references indexed in Scilit:
- Overexpression, purification, and mechanistic study of UDP-N-acetylenolpyruvylglucosamine reductaseBiochemistry, 1993
- Cloning and sequencing of Escherichia coli murZ and purification of its product, a UDP-N-acetylglucosamine enolpyruvyl transferaseJournal of Bacteriology, 1992
- Cloning and identification of the Escherichia coli murB DNA sequence, which encodes UDP-N-acetylenolpyruvoylglucosamine reductaseJournal of Bacteriology, 1992
- Intracellular steps of bacterial cell wall peptidoglycan biosynthesis: enzymology, antibiotics, and antibiotic resistanceNatural Product Reports, 1992
- Sparse matrix sampling: a screening method for crystallization of proteinsJournal of Applied Crystallography, 1991
- A system for collection and on-line integration of X-ray diffraction data from a multiwire area detectorJournal of Applied Crystallography, 1987