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Crystallization and preliminary X-ray analysis of a UDP-MurNAc-tripeptide D -alanyl- D -alanine-adding enzyme (PaMurF) from Pseudomonas aeruginosa

DOI: 10.1107/S1744309113005344 DOI Help

Authors: Vita Majce (University of Warwick) , Karen Ruane (University of Warwick) , Stanislav Gobec (University of Ljubljana) , David Roper (University of Warwick)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Acta Crystallographica Section F Structural Biology And Crystallization Communications , VOL 69 (5) , PAGES 503 - 505

State: Published (Approved)
Published: May 2013
Diamond Proposal Number(s): 8359

Abstract: The ATP-dependent UDP-MurNAc-tripeptide: d-Ala-d-Ala ligase MurF catalyses the last step in the cytoplasmic phase of peptidoglycan biosynthesis, which is critical in the formation of the bacterial cell wall and in the recycling of peptidoglycan intermediates. In this study, the crystallization of MurF from the Gram-negative pathogen Pseudomonas aeruginosa in the presence of its UDP-MurNAc-tripeptide substrate is reported. The crystals belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 57.81, b = 87.29, c = 92.61 angstrom, and data were collected to 1.92 angstrom resolution, allowing study of the enzyme in the substrate-liganded form for the first time.

Journal Keywords: MurF; peptidoglycan; Pseudomonas aeruginosa.

Diamond Keywords: Bacteria; Enzymes

Subject Areas: Biology and Bio-materials

Instruments: I04-1-Macromolecular Crystallography (fixed wavelength)

Added On: 11/03/2016 14:16

Discipline Tags:

Pathogens Health & Wellbeing Structural biology Life Sciences & Biotech

Technical Tags:

Diffraction Macromolecular Crystallography (MX)