PDBsum entry 1v7b

Gene reguration

PDB id: 1v7b

Contents

Protein chains

175 a.a. *

Waters ×154

* Residue conservation analysis

Superseded by:

2zoy

PDB id:

1v7b

Name:

Gene reguration

Title:

Tetr-family transcription factor cgl2612 from c.Glutamicum

Structure:

Transcriptional regulator. Chain: a, b. Synonym: cgl2612 protein. Engineered: yes

Source:

Corynebacterium glutamicum atcc 13032. Strain: atcc 13032. Expressed in: escherichia coli.

Biol. unit:

Dimer (from PQS)

Resolution:

1.90Å R-factor: 0.208 R-free: 0.241

Authors:

H.Itou,M.Yao,N.Watanabe,I.Tanaka

Key ref:

H.Itou et al. (2005). The CGL2612 protein from Corynebacterium glutamicum is a drug resistance-related transcriptional repressor: structural and functional analysis of a newly identified transcription factor from genomic DNA analysis. J Biol Chem, 280, 38711-38719. PubMed id: 16166084 DOI: 10.1074/jbc.M505999200

Date:

16-Dec-03 Release date: 18-Jan-05

Protein chains

Q8NMG3  (Q8NMG3_CORGL) -  Transcriptional regulator from Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025)

Seq: 177 a.a.

Struc: 175 a.a.

DOI no: 10.1074/jbc.M505999200

J Biol Chem 280:38711-38719 (2005)

PubMed id: 16166084

The CGL2612 protein from Corynebacterium glutamicum is a drug resistance-related transcriptional repressor: structural and functional analysis of a newly identified transcription factor from genomic DNA analysis.

H.Itou, U.Okada, H.Suzuki, M.Yao, M.Wachi, N.Watanabe, I.Tanaka.

ABSTRACT

The emergence of antibiotic-resistant bacteria often causes serious clinical problems. The TetR family is one of the major transcription factor families that regulate expression of genes involved in bacterial antimicrobial resistance systems. CGL2612 protein is a transcription factor newly identified by genomic DNA analysis on Corynebacterium glutamicum, which belongs to the mycolic acid-containing Actinomycetales, including the well known pathogens Corynebacterium diphtheriae and Mycobacterium tuberculosis. Crystal structure analysis showed that the CGL2612 protein exhibits significant structural similarity to the multidrug resistance (MDR)-related transcription factor QacR from Staphylococcus aureus, despite poor amino acid sequence similarity between these proteins. Binding DNA sequence analysis of CGL2612 protein using the systematic evolution of ligands by the exponential enrichment (systematic evolution of ligands by exponential enrichment, or SELEX) method revealed that this protein is a new member of the TetR family, which regulates expression of the immediately upstream gene, cgl2611, probably encoding a major facilitator superfamily permease. Subsequent functional analyses confirmed a function of the CGL2612 as a transcriptional repressor responsible for the antimicrobial resistance system in C. glutamicum. The strategy used in the present study is one of the most convenient and powerful methods to analyze functionally unknown transcription factors, and the results obtained here will contribute to our understanding of the drug resistance mechanism not only in C. glutamicum but also in the related bacteria, C. diphtheriae and M. tuberculosis.

Selected figure(s)

Figure 1.
FIGURE 1. Ribbon representation of CGL2612 dimer. Each subunit is shown in gray and white. Ribbon representations appearing in this figure and Fig. 5b were generated using the MOLSCRIPT (30) and RASTER3D (31) programs.

Figure 4.
FIGURE 4. Top, schematic representation of the structures of cgl2611 and cgl2612 genes and the cgl2611 promoter region. Bottom, sequence representation of the DNA fragments isolated by genomic and random SELEX analysis. In genomic SELEX, the consensus sequence composed of all isolated fragments is represented in boldface type. In random SELEX, positions homologous to the consensus sequence are highlighted in boldface type. The opposing two arrows indicate the half-site of the pseudoinverted-repeat sequence observed here. *, the symmetry center of the palindrome.

The above figures are reprinted by permission from the ASBMB: J Biol Chem (2005, 280, 38711-38719) copyright 2005.

Figures were selected by an automated process.