FolX from Pseudomonas aeruginosa is octameric in both crystal and solution

Gabrielsen, M. , Beckham, K.S.H., Cogdell, R.J. , Byron, O. and Roe, A.J. (2012) FolX from Pseudomonas aeruginosa is octameric in both crystal and solution. FEBS Letters, 586(8), pp. 1160-1165. (doi: 10.1016/j.febslet.2012.03.031) (PMID:22575651) (PMCID:PMC3405516)

Abstract

FolX encodes an epimerase that forms one step of the tetrahydrofolate biosynthetic pathway, which is of interest as it is an established target for important drugs. Here we report the crystal structure of FolX from the bacterial opportunistic pathogen Pseudomonas aeruginosa, as well as a detailed analysis of the protein in solution, using analytical ultracentrifugation (AUC) and small-angle X-ray scattering (SAXS). In combination, these techniques confirm that the protein is an octamer both in the crystal structure, and in solution.

• Item Type: Articles
• Additional Information: NOTICE: this is the author’s version of a work that was accepted for publication in FEBS Letters. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in FEBS Letters, http://dx.doi.org/10.1016/j.febslet.2012.03.031
• Status: Published
• Refereed: Yes
• Glasgow Author(s) Enlighten ID: Gabrielsen, Dr Mads and Roe, Professor Andrew and Byron, Professor Olwyn and Cogdell, Professor Richard
• Authors: Gabrielsen, M., Beckham, K.S.H., Cogdell, R.J., Byron, O., and Roe, A.J.
• College/School: College of Medical Veterinary and Life Sciences > School of Infection & Immunity
• Journal Name: FEBS Letters
• Publisher: Elsevier
• ISSN: 0014-5793
• Copyright Holders: Copyright © 2012 Elsevier
• First Published: First published in FEBS Letters
• Publisher Policy: Reproduced in accordance with the copyright policy of the publisher

Project Code	Award No	Project Name	Principal Investigator	Funder's Name	Funder Ref	Lead Dept
49144	1	A biochemical and molecular analysis of the YhaO membrane protein in Escherichia coli O157:H7	Andrew Roe	Biotechnology and Biological Sciences Research Council (BBSRC)	BB/G011389/1	Infection Immunity and Inflammation Life Sciences