PDBsum entry: 2gxg

Transcription

PDB id: 2gxg

Contents

Protein chain

140 a.a. *

Waters ×124

* Residue conservation analysis

PDB id:

2gxg

Name:

Transcription

Title:

Crystal structure of emrr homolog from hyperthermophilic arc sulfolobus tokodaii strain7

Structure:

146aa long hypothetical transcriptional regulator chain: a. Synonym: transcriptional repressor protein. Engineered: yes

Source:

Sulfolobus tokodaii. Organism_taxid: 111955. Strain: strain7. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

1.45Å R-factor: 0.223 R-free: 0.239

Authors:

K.Miyazono,M.Tsujimura,Y.Kawarabayasi,M.Tanokura

Key ref:

K.Miyazono et al. (2007). Crystal structure of an archaeal homologue of multidrug resistance repressor protein, EmrR, from hyperthermophilic archaea Sulfolobus tokodaii strain 7. Proteins, 67, 1138-1146. PubMed id: 17357153 DOI: 10.1002/prot.21327

Date:

08-May-06 Release date: 20-Mar-07

Protein chain

Q96ZY1  (Q96ZY1_SULTO) -  Putative MarR family transcriptional regulator

Seq: 146 a.a.

Struc: 140 a.a.

 Gene Ontology (GO) functional annotation 

• Cellular component: intracellular (1 term)
• Biological process: transcription, DNA-dependent (2 terms)
• Biochemical function: DNA binding (2 terms)

DOI no: 10.1002/prot.21327

Proteins 67:1138-1146 (2007)

PubMed id: 17357153

Crystal structure of an archaeal homologue of multidrug resistance repressor protein, EmrR, from hyperthermophilic archaea Sulfolobus tokodaii strain 7.

K.Miyazono, M.Tsujimura, Y.Kawarabayasi, M.Tanokura.

ABSTRACT

MarR family proteins, MarR, MexR, and EmrR, are known as bacterial regulators for a phenotype resistant to multiple antibiotic drugs. Genomic data have indicated the presence of bacterial-type transcriptional regulators, including MarR family proteins in archaea, though the archaeal transcription system is close to that of eukaryote. To elucidate the structural basis of the transcriptional regulation mechanism of archaeal MarR family proteins, the crystal structure of the ST1710 protein, which was identified as an archaeal EmrR homologue, StEmrR, from hyperthermophilic archaeon Sulfolobus tokodaii strain 7 was determined at 1.45-A resolution. The protein was composed of two N- and C-terminal dimerization domains, and the DNA-binding domain consisted of a winged helix motif, as in the case of bacterial MarR family proteins. Despite the relatively low overall structural similarity between StEmrR and bacterial MarR family proteins, the structure of the DNA-binding domain displayed high structural similarity. A comparison with the crystal structures of bacterial MarR family proteins revealed that structural variation was mainly due to the different orientation of the two helices at the N- and C-termini. Our results indicated that the distance between the two DNA-binding domains of MarR family proteins would be changed by the rotation of the two terminal helices to interact with the target DNA.

Selected figure(s)

Figure 2.
Figure 2. Structure of StEmrR. (a) A ribbon diagram of the monomer structure of StEmrR. Color coding runs from blue at the N-terminal region to red at the C-terminal region. Secondary structure assignments are labeled on the ribbon model. (b) A ribbon diagram of the dimer structure of StEmrR. The dimerization domain is shown by red and gray ribbon model, and the DNA-binding domain is shown by a blue ribbon model. (c) Inter subunit interactions of the StEmrR dimer. Residues involved in hydrophobic interactions are shown in a black sphere model, and those involved in inter subunit salt bridge formation are shown in blue (positively charged residues) and red (negatively charged residues) stick models. The dotted lines show inter-subunit salt bridges. (d) Position and interactions of highly conserved Gly78, Thr97, and Gly100. Dotted line shows hydrogen bonds between these residues.

Figure 3.
Figure 3. Comparison of the monomer structure of StEmrR with the structures of other MarR family proteins. (a) Stereo diagram of superposed monomer structures of StEmrR and bacterial MarR family proteins (MarR and MexR-C) using the C atoms of their DNA-binding domains. StEmrR, MarR, and MexR-C are show in red, green, and blue, respectively. (b) Stereo diagram of the superposed structures rotated by 90°. The structural variations of this family are primarily caused by the different orientation of helices 1 and 6.

The above figures are reprinted by permission from John Wiley & Sons, Inc.: Proteins (2007, 67, 1138-1146) copyright 2007.

Figures were selected by an automated process.