Crystallization of the N‐terminal regulatory domain of the enhancer‐binding protein FleQ from Stenotrophomonas maltophilia. Issue 3 (1st March 2014)

• Record Type: Journal Article
• Authors: Yang, Jauo‐Guey; Shih, Min‐Shao; Kuo, Wei‐Ting; Chin, Ko‐Hsin; Shen, Gwan‐Han; Chou, Shan‐Ho
• Is Part Of: Acta crystallographica. Volume 70:Issue 3(2014:Mar.)
• Page Start: 326
• Page End: 330
• Publication Date: 2014-03-01
• Subjects: Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S2053230X14001514
• Languages: English
• ISSNs: 2053-230X

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>FleQ is a master regulator that controls bacterial flagellar gene expression. It is a unique enhancer‐binding protein or repressor protein comprising an N‐terminal FleQ domain, an AAA⁺/ATPase σ54‐interaction domain and a helix–turn–helix DNA‐binding domain. FleN is a putative ATPase with a deviant Walker A motif that works together with FleQ by binding to the FleQ N‐terminal domain to fully express <italic>pel</italic>, <italic>psl</italic> and <italic>cdr</italic> operons in the presence of c‐di‐GMP to enhance biofilm formation. <italic>Stenotrophomonas maltophilia</italic> is an emerging human pathogen that causes fatal infections in humans. In order to understand the interaction between the FleN and FleQ domains and its effect on <italic>S. maltophilia</italic> biofilm formation, determination of the FleQ–c‐di‐GMP and FleN–FleQ–c‐di‐GMP complex structures was embarked upon. Towards this goal, the FleQ N‐terminal domain from <italic>S. maltophilia</italic> was first cloned and expressed in <italic>Escherichia coli</italic>. Native and SeMet‐labelled FleQ domains were successfully crystallized and diffracted to resolutions of 2.08 and 2.58 Å, respectively.</p> </abstract>