Crystallization and preliminary X‐ray analysis of the periplasmic domain of FliP, an integral membrane component of the bacterial flagellar type III protein‐export apparatus. Issue 9 (1st September 2014)

• Record Type: Journal Article
• Authors: Fukumura, Takuma; Furukawa, Yukio; Kawaguchi, Tatsuya; Saijo‐Hamano, Yumiko; Namba, Keiichi; Imada, Katsumi; Minamino, Tohru
• Is Part Of: Acta crystallographica. Volume 70:Issue 9(2014:Sep.)
• Page Start: 1215
• Page End: 1218
• Publication Date: 2014-09-01
• Subjects: Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S2053230X14014678
• Languages: English
• ISSNs: 2053-230X

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>The bacterial flagellar proteins are transported <italic>via</italic> a specific export apparatus to the distal end of the growing structure for their self‐assembly. FliP is an essential membrane component of the export apparatus. FliP has an N‐terminal signal peptide and is predicted to have four transmembrane (TM) helices and a periplasmic domain (FliP_P) between TM‐2 and TM‐3. In this study, FliP_P from <italic>Thermotoga maritima</italic> (TmFliP_P) and its selenomethionine derivative (SeMet‐TmFliP_P) were purified and crystallized. TmFliP_P formed a homotetramer in solution. Crystals of TmFliP_P and SeMet‐TmFliP_P were obtained by the hanging‐drop vapour‐diffusion technique with 2‐methyl‐2, 4‐pentanediol as a precipitant. These two crystals grew in the hexagonal space group <italic>P</italic>6₂22 or <italic>P</italic>6₄22, with unit‐cell parameters <italic>a</italic> = <italic>b</italic> = 114.9, <italic>c</italic> = 193.8 Å. X‐ray diffraction data were collected from crystals of TmFliP_P and SeMet‐TmFliP_P to 2.4 and 2.8 Å resolution, respectively.</p> </abstract>