Crystal Structure of the Full-Length Sorbitol Operon Regulator SorC from Klebsiella pneumoniae: Structural Evidence for a Novel Transcriptional Regulation Mechanism

• Published in: Journal of molecular biology Vol. 387; no. 3; pp. 759 - 770
• Main Authors: de Sanctis, Daniele, McVey, Colin E., Enguita, Francisco J., Carrondo, Maria Armenia
• Format: Journal Article
• Language: English
• Published: England Elsevier Ltd 03.04.2009
• Subjects: Bacterial Proteins - chemistry; Bacterial Proteins - genetics; Bacterial Proteins - metabolism; Crystallography, X-Ray; Gene Expression Regulation, Bacterial; Klebsiella pneumoniae; Klebsiella pneumoniae - genetics; Klebsiella pneumoniae - metabolism; Models, Molecular; Molecular Sequence Data; Operator Regions, Genetic; Operon; Protein Multimerization; Protein Structure, Quaternary; Protein Subunits - chemistry; Protein Subunits - genetics; Protein Subunits - metabolism; Sorbitol - chemistry; Sorbitol - metabolism; sorbitol operon regulator; SorC; Transcription Factors - chemistry; Transcription Factors - genetics; Transcription Factors - metabolism; transcriptional regulation; X-ray crystallography; MPD; sorbitol operon regulator; X-ray crystallography; SRD; transcriptional regulation; DBD; SorC; HTH; Klebsiella pneumoniae; PDB; CggR

SorC transcriptional regulators are common regulators in prokaryotes. Here we report the first crystal structure of a full-length SorC, the sorbitol operon regulator SorC from Klebsiella pneumoniae, the prototype of its family. SorC was found to be a homotetramer (which seems to be the biologically...