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Crystal structure of an Lrs14‐like archaeal biofilm regulator from Sulfolobus acidocaldarius
Author(s) -
Vogt Marian S.,
Völpel Simon L.,
Albers Sonja-Verena,
Essen Lars-Oliver,
Banerjee Ankan
Publication year - 2018
Publication title -
acta crystallographica section d
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.374
H-Index - 138
ISSN - 2059-7983
DOI - 10.1107/s2059798318014146
Subject(s) - sulfolobus acidocaldarius , antiparallel (mathematics) , dimer , crystal structure , protein structure , crystallography , archaea , biology , helix (gastropod) , chemistry , stereochemistry , genetics , biochemistry , gene , physics , organic chemistry , quantum mechanics , magnetic field , ecology , snail
The small winged helix–turn–helix (wHTH) proteins of the Lrs14 family are major transcriptional regulators and act as archaeal biofilm regulators (AbfRs) in the crenarchaeote Sulfolobus acidocaldarius . Here, the first crystal structure of an AbfR ortholog, AbfR2, the deletion of which is known to impair biofilm formation, is presented. Like most other wHTH orthologs, AbfR2 is dimeric in solution as well as in its 2.45 Å resolution crystal structure. Given the presence of three independent AbfR2 dimers in the asymmetric unit, the crystal structure shows a considerable degree of conformational variation within the dimer, the antiparallel orientations of which are stabilized by coiled‐coil interaction between H4 helices. Conserved anchor interactions between helices H0 and H4 of AbfR2 further contribute to dimer stabilization. The combined structural and bioinformatic analysis reveals cluster‐specific structural differences between different members of the Lrs14 protein family.