Crystallization and preliminary X-ray analysis of BigR, a transcription repressor from Xylella fastidiosa involved in biofilm formation.
BigR (biofilm growth-associated repressor) is a novel repressor protein that regulates the transcription of an operon implicated in biofilm growth in both Xylella fastidiosa and Agrobacterium tumefaciens. This protein binds to a palindromic TA-rich element located in the promoter of the BigR operon and strongly represses transcription of the operon. BigR contains a helix-turn-helix (HTH) domain that is found in some members of the ArsR/SmtB family of metal sensors, which control metal resistance in bacteria. Although functional studies have suggested that BigR does not act as a metal sensor, the presence of two cysteines and a methionine in its primary structure raised the possibility of BigR being a metal-ligand protein. In order to gain new insights into the protein structure and its possible interaction with a metal ion or effector ligand, BigR from X. fastidiosa was crystallized in native and selenomethionine (SeMet) labelled forms using the hanging-drop vapour-diffusion method. X-ray diffraction data were collected from native and SeMet crystals to resolutions of 1.95 and 2.2 A, respectively. Both crystals belong to space group P321 and contain one molecule per asymmetric unit.
Barbosa
Rosicler Lázaro
RL
Center for Molecular and Structural Biology, Brazilian Synchrotron Light Laboratory, Campinas, SP, CP 6192, CEP 13083-970, Brazil.
Rinaldi
Fábio Cupri
FC
Guimarães
Beatriz Gomes
BG
Benedetti
Celso Eduardo
CE
D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics; D018441:Biofilms / Q000254:growth & development*; D003460:Crystallization; D014157:Transcription Factors / Q000737:chemistry / Q000235:genetics; D014158:Transcription, Genetic; D014961:X-Ray Diffraction; D044167:Xylella / Q000737:chemistry* / Q000235:genetics
D001426:Bacterial Proteins; D014157:Transcription Factors