2ZCW

Crystal Structure of TTHA1359, a Transcriptional Regulator, CRP/FNR family from Thermus thermophilus HB8

Replaces:  2COH

Summary for 2ZCW

• Entry DOI: 10.2210/pdb2zcw/pdb
• Descriptor: Transcriptional regulator, FNR/CRP family, (4S)-2-METHYL-2,4-PENTANEDIOL (3 entities in total)
• Functional Keywords: fnr/crp family, transcriptional regulator, thermus thermophilus, stationary phase, dna-binding, transcription regulation, winged helix dna-binding domain, camp-binding domain, structural genomics, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi, transcription
• Biological source: Thermus thermophilus
• Total number of polymer chains: 1
• Total formula weight: 22749.87

Authors

Agari, Y.,Yokoyama, S.,Kuramitsu, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2007-11-13, release date: 2007-12-04, Last modification date: 2011-07-13)

Primary citation

Agari, Y.,Kashihara, A.,Yokoyama, S.,Kuramitsu, S.,Shinkai, A.
Global gene expression mediated by Thermus thermophilus SdrP, a CRP/FNR family transcriptional regulator
Mol.Microbiol., 70:60-75, 2008

PubMed Abstract: Thermus thermophilus SdrP is one of four cyclic AMP receptor protein (CRP)/fumarate and nitrate reduction regulator (FNR) family proteins from the extremely thermophilic bacterium T. thermophilus HB8. Expression of sdrP mRNA increased in the stationary phase during cultivation at 70 degrees C. Although the sdrP gene was non-essential, an sdrP-deficient strain showed growth defects, particularly when grown in a synthetic medium, and increased sensitivity to disulphide stress. The expression of several genes was altered in the sdrP disruptant. Among them, we found eight SdrP-dependent promoters using in vitro transcription assays. A predicted SdrP binding site similar to that recognized by Escherichia coli CRP was found upstream of each SdrP-dependent promoter. In the wild-type strain, expression of these eight genes tended to increase upon entry into the stationary phase. Transcriptional activation in vitro was independent of any added effector molecule. The hypothesis that apo-SdrP is the active form of the protein was supported by the observation that the three-dimensional structure of apo-SdrP is similar to that of the DNA-binding form of E. coli CRP. Based on the properties of the SdrP-regulated genes found in this study, it is speculated that SdrP is involved in nutrient and energy supply, redox control, and polyadenylation of mRNA.

PubMed: 18699868
DOI: 10.1111/j.1365-2958.2008.06388.x

Experimental method

X-RAY DIFFRACTION (1.5 Å)