title: Crystal structure of the single-stranded RNA binding protein HutP from Geobacillus thermodenitrificans.
abstract: RNA binding proteins control gene expression by the attenuation/antitermination mechanism. HutP is an RNA binding antitermination protein. It regulates the expression of hut operon when it binds with RNA by modulating the secondary structure of single-stranded hut mRNA. HutP necessitates the presence of l-histidine and divalent metal ion to bind with RNA. Herein, we report the crystal structures of ternary complex (HutP-l-histidine-Mg(2+)) and EDTA (0.5 M) treated ternary complex (HutP-l-histidine-Mg(2+)), solved at 1.9 Å and 2.5 Å resolutions, respectively, from Geobacillus thermodenitrificans. The addition of 0.5 M EDTA does not affect the overall metal-ion mediated ternary complex structure and however, the metal ions at the non-specific binding sites are chelated, as evidenced from the results of structural features.
authors.affiliation: Centre of Advanced Study in Crystallography and Biophysics, University of Madras, Guindy Campus, Chennai 600 025, India.
authors.forename: Viswanathan
authors.initials: V
authors.lastname: Thiruselvam
authors.affiliation: RIKEN SPring-8 Center, Harima Institute, 1-1-1 Kuoto, Sayo, Hyogo 679-5148, Japan.
authors.forename: Padavattan
authors.initials: P
authors.lastname: Sivaraman
authors.affiliation: RIKEN SPring-8 Center, Harima Institute, 1-1-1 Kuoto, Sayo, Hyogo 679-5148, Japan; Structural Biology Laboratory, RIKEN Yokohama Institute, RIKEN, 1-7-22 Suehiro-cho, Tsurumi, Yokohama 230-0045, Japan. Electronic address: Kumarevel.thirumananseri@riken.jp.
authors.forename: Thirumananseri
authors.initials: T
authors.lastname: Kumarevel
authors.affiliation: Centre of Advanced Study in Crystallography and Biophysics, University of Madras, Guindy Campus, Chennai 600 025, India. Electronic address: mnpsy@hotmail.com.
authors.forename: Mondikalipudur Nanjappagounder
authors.initials: MN
authors.lastname: Ponnuswamy
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D001665:Binding Sites; D018360:Crystallography, X-Ray; D056506:Geobacillus / Q000737:chemistry* / Q000378:metabolism; D006639:Histidine / Q000737:chemistry / Q000378:metabolism; D008274:Magnesium / Q000737:chemistry / Q000378:metabolism; D008958:Models, Molecular; D011487:Protein Conformation; D012333:RNA, Messenger / Q000378:metabolism; D016601:RNA-Binding Proteins / Q000737:chemistry* / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; D012333:RNA, Messenger; D016601:RNA-Binding Proteins; D006639:Histidine; D008274:Magnesium
keywords: Antitermination; Gene regulation; Geobacillus thermodenitrificans; HutP; RNA binding