Crystal structure of TM1030 from Thermotoga maritima at 2.3 angstrom resolution reveals molecular details of its transcription repressor function

Premkumar, Lakshmanane, Rife, Christopher L., Krishna, S. Sri, McMullan, Daniel, Miller, Mitchell D., Abdubek, Polat, Ambing, Eileen, Astakhova, Tamara, Axelrod, Herbert L., Canaves, Jaume M., Carlton, Dennis, Chiu, Hsiu-Ju, Clayton, Thomas, DiDonato, Michael, Duan, Lian, Elsliger, Marc-André, Feuerhelm, Julie, Floyd, Ross, Grzechnik, Slawomir K., Hale, Joanna, Hampton, Eric, Han, Gye Won, Haugen, Justin, Jaroszewski, Lukasz, Jin, Kevin K., Klock, Heath E., Knuth, Mark W., Koesema, Eric, Kovarik, John S., Kreusch, Andreas, Levin, Inna, McPhillips, Timothy M., Morse, Andrew T., Nigoghossian, Edward, Okach, Linda, Oommachen, Silvya, Paulsen, Jessica, Quijano, Kevin, Reyes, Ron, Rezezadeh, Fred, Rodionov, Dmitry, Schwarzenbacher, Robert, Spraggon, Glen, van den Bedem, Henry, White, Aprilfawn, Wolf, Guenter, Xu, Qingping, Hodgson, Keith O., Wooley, John, Deacon, Ashley M., Godzik, Adam, Lesley, Scott A. and Wilson, Ian A. (2007) Crystal structure of TM1030 from Thermotoga maritima at 2.3 angstrom resolution reveals molecular details of its transcription repressor function. Proteins: Structure, Function and Bioinformatics, 68 1: 418-424. doi:10.1002/prot.21436


Author Premkumar, Lakshmanane
Rife, Christopher L.
Krishna, S. Sri
McMullan, Daniel
Miller, Mitchell D.
Abdubek, Polat
Ambing, Eileen
Astakhova, Tamara
Axelrod, Herbert L.
Canaves, Jaume M.
Carlton, Dennis
Chiu, Hsiu-Ju
Clayton, Thomas
DiDonato, Michael
Duan, Lian
Elsliger, Marc-André
Feuerhelm, Julie
Floyd, Ross
Grzechnik, Slawomir K.
Hale, Joanna
Hampton, Eric
Han, Gye Won
Haugen, Justin
Jaroszewski, Lukasz
Jin, Kevin K.
Klock, Heath E.
Knuth, Mark W.
Koesema, Eric
Kovarik, John S.
Kreusch, Andreas
Levin, Inna
McPhillips, Timothy M.
Morse, Andrew T.
Nigoghossian, Edward
Okach, Linda
Oommachen, Silvya
Paulsen, Jessica
Quijano, Kevin
Reyes, Ron
Rezezadeh, Fred
Rodionov, Dmitry
Schwarzenbacher, Robert
Spraggon, Glen
van den Bedem, Henry
White, Aprilfawn
Wolf, Guenter
Xu, Qingping
Hodgson, Keith O.
Wooley, John
Deacon, Ashley M.
Godzik, Adam
Lesley, Scott A.
Wilson, Ian A.
Title Crystal structure of TM1030 from Thermotoga maritima at 2.3 angstrom resolution reveals molecular details of its transcription repressor function
Formatted title
Crystal structure of TM1030 from Thermotoga maritima at 2.3 Å resolution reveals molecular details of its transcription repressor function
Journal name Proteins: Structure, Function and Bioinformatics   Check publisher's open access policy
ISSN 0887-3585
1097-0134
Publication date 2007-07
Sub-type Article (original research)
DOI 10.1002/prot.21436
Volume 68
Issue 1
Start page 418
End page 424
Total pages 7
Place of publication Hoboken, NJ, U.S.A.
Publisher John Wiley & Sons
Language eng
Formatted abstract
Transcriptional regulators play a crucial role in the adaptation of microorganisms to diverse environmental challenges. Most microbial transcriptional regulators contain an effector binding regulatory domain and a DNA-binding domain that interacts with a specific operator DNA to either prevent (transcriptional repressors) or stimulate (transcriptional activators) transcription of a nearby gene(s). Prokaryotic transcriptional regulators have been classified into a number of families based on amino acid sequence similarity and domain architecture.

The tetracycline repressor (TetR) family of proteins exhibits a high degree of sequence similarity at the N-terminal DNA-binding domain (∼50 amino acids), which adopts a helix-turn-helix (HTH) motif. In contrast, the regulatory domain is more variable, possibly reflecting the need to specifically accommodate different effectors. TM1030 from Thermotoga maritima, a hyperthermophilic bacterium that typically thrives in high temperature ecosystems, is a 200 amino acid protein with a molecular weight of 24 kDa and an isoelectric point of 6.25. The N-terminal DNA-binding domain of TM1030 shows sequence similarity to members of the TetR family, but no significant similarity is found for the regulatory C-terminal region (∼150 amino acids). Here, we present the crystal structure of a ligand-bound form of TM1030, which was determined to 2.3 Å resolution, using the semiautomated, high-throughput pipeline of the Joint Center for Structural Genomics (JCSG) as part of the National Institute of General Medical Sciences (NIGMS)- funded Protein Structure Initiative (PSI).
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collection: Institute for Molecular Bioscience - Publications
 
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Created: Tue, 06 Sep 2011, 09:51:21 EST by Susan Allen on behalf of Institute for Molecular Bioscience