7acm

Crystal structure of E. coli HTH-type transcriptional regulator RcdA in complex with TMAO at 1.76 A resolution

spinqualitylabelsall models 7acm, resolution 1.76Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7acm is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.763Å Ligands: TMO Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function RCDA_ECOLI Regulates the expression of a number of genes involved in biofilm formation and stress response. Target genes include six stress-response transcriptional regulators: csgD, which is a master regulator of biofilm formation, appY, sxy, ycgF, fimB and rcdA itself. This indicates that a large number of genes must be regulated indirectly via these transcriptional regulators. Acts by binding to the upstream region of its target genes. Publication Abstract from PubMed RcdA is a helix-turn-helix (HTH) transcriptional regulator belonging to the TetR family. The protein regulates the transcription of curlin subunit gene D, the master regulator of biofilm formation. Moreover, it was predicted that it might be involved in the regulation of up to 27 different genes. However, an effector of RcdA and the environmental conditions which trigger RcdA action remain unknown. Herein, we report the first crystal structures of RcdA in complexes with ligands, trimethylamine N-oxide (TMAO) and tris(hydroxymethyl)aminomethane (Tris), which might serve as RcdA effectors. Based on these structures, the ligand-binding pocket of RcdA was characterized in detail. The conservation of the amino acid residues forming the ligand-binding cavity was analyzed and the comprehensive search for RcdA structural homologs was performed. This analysis indicated that RcdA is structurally similar to multidrug-binding TetR family members, however, its ligand-binding cavity differs significantly from the pockets of its structural homologs. The interaction of RcdA with TMAO and Tris indicates that the protein might be involved in alkaline stress response. Structures of the TetR-like transcription regulator RcdA alone and in complexes with ligands.,Pietrzyk-Brzezinska AJ, Cociurovscaia A Proteins. 2021 Jul 20. doi: 10.1002/prot.26183. PMID:34288132 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also RcdA Tetracycline repressor protein 3D structures

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