6CMV

Crystal structure of Archaeal Biofilm Regulator (AbfR2) from Sulfolobus acidocaldarius

Summary for 6CMV

• Entry DOI: 10.2210/pdb6cmv/pdb
• Descriptor: Transcriptional regulator Lrs14-like protein, GLYCEROL, (4S)-2-METHYL-2,4-PENTANEDIOL, ... (4 entities in total)
• Functional Keywords: whth, archaea, biofilm, gene regulation
• Biological source: Sulfolobus acidocaldarius
• Total number of polymer chains: 6
• Total formula weight: 101163.63

Authors

Essen, L.-O.,Vogt, M.S.,Banerjee, A. (deposition date: 2018-03-06, release date: 2018-11-14, Last modification date: 2024-11-13)

Primary citation

Vogt, M.S.,Volpel, S.L.,Albers, S.V.,Essen, L.O.,Banerjee, A.
Crystal structure of an Lrs14-like archaeal biofilm regulator from Sulfolobus acidocaldarius.
Acta Crystallogr D Struct Biol, 74:1105-1114, 2018

PubMed Abstract: 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.

PubMed: 30387769
DOI: 10.1107/S2059798318014146

Experimental method

X-RAY DIFFRACTION (2.45 Å)