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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
Majce, Vita (Author), Ruane, Karen M. (Author), Gobec, Stanislav (Author), Roper, David I. (Author)

URLURL - Presentation file, Visit http://onlinelibrary.wiley.com/doi/10.1107/S1744309113005344/pdf This link opens in a new window

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 P212121, with unit-cell parameters a = 57.81, b = 87.29, c = 92.61 Å, and data were collected to 1.92 Å resolution, allowing study of the enzyme in the substrate-liganded form for the first time

Language:English
Keywords:MurF, peptidoglikan, Pseudomonas aeruginosa, biosinteza, kristalizacija
Work type:Not categorized (r6)
Tipology:1.03 - Short Scientific Article
Organization:FFA - Faculty of Pharmacy
Year:2013
Number of pages:str. 503-505
Numbering:Vol. F69, no. 5
UDC:543:548.3
ISSN on article:1744-3091
DOI:10.1107/S1744309113005344 Link is opened in a new window
COBISS.SI-ID:3479921 Link is opened in a new window
Views:302
Downloads:150
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Record is a part of a journal

Title:Acta crystallographica
Publisher:International Union of Crystallography
ISSN:1744-3091
COBISS.SI-ID:20224985 This link opens in a new window

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