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X-ray crystallographic studies of tr...

Benoff, Brian Eric.

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X-ray crystallographic studies of transcription regulation: Activation: The CAP-alphaCTD-DNA complex. Repression: The tryptophan repressor.

Record Type:	Electronic resources : Monograph/item
Title/Author:	X-ray crystallographic studies of transcription regulation: Activation: The CAP-alphaCTD-DNA complex. Repression: The tryptophan repressor./
Author:	Benoff, Brian Eric.
Description:	287 p.
Notes:	Source: Dissertation Abstracts International, Volume: 64-06, Section: B, page: 2648.
Contained By:	Dissertation Abstracts International64-06B.
Subject:	Chemistry, Biochemistry. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3092916

X-ray crystallographic studies of transcription regulation: Activation: The CAP-alphaCTD-DNA complex. Repression: The tryptophan repressor.
Benoff, Brian Eric.

X-ray crystallographic studies of transcription regulation: Activation: The CAP-alphaCTD-DNA complex. Repression: The tryptophan repressor. - 287 p.

Source: Dissertation Abstracts International, Volume: 64-06, Section: B, page: 2648.

Thesis (Ph.D.)--Rutgers The State University of New Jersey - New Brunswick, 2003.

This dissertation presents four crystal structure determinations of proteins that are capable of forming protein-DNA complexes. One structure is the <italic> E. coli</italic> Catabolite gene Activator Protein (CAP) in complex with the C-terminal domain of alpha (αCTD) from RNA polymerase (RNAP) and DNA. In addition, three structures of the Tryptophan (Trp) repressor without DNA are presented: <italic>wt</italic> apo-repressor, a temperature sensitive mutant (L75F), and <italic>wt</italic> in a domain-swapped supramolecular array.Subjects--Topical Terms:

1017722
Chemistry, Biochemistry.

X-ray crystallographic studies of transcription regulation: Activation: The CAP-alphaCTD-DNA complex. Repression: The tryptophan repressor.
LDR:03243nmm 2200301 4500 001 1859372
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035 $a (UnM)AAI3092916
035 $a AAI3092916
040 $a UnM $c UnM
100 1 $a Benoff, Brian Eric. $3 1947032
245 1 0 $a X-ray crystallographic studies of transcription regulation: Activation: The CAP-alphaCTD-DNA complex. Repression: The tryptophan repressor.
300 $a 287 p.
500 $a Source: Dissertation Abstracts International, Volume: 64-06, Section: B, page: 2648.
500 $a Director: Helen M. Berman.
502 $a Thesis (Ph.D.)--Rutgers The State University of New Jersey - New Brunswick, 2003.
520 $a This dissertation presents four crystal structure determinations of proteins that are capable of forming protein-DNA complexes. One structure is the <italic> E. coli</italic> Catabolite gene Activator Protein (CAP) in complex with the C-terminal domain of alpha (αCTD) from RNA polymerase (RNAP) and DNA. In addition, three structures of the Tryptophan (Trp) repressor without DNA are presented: <italic>wt</italic> apo-repressor, a temperature sensitive mutant (L75F), and <italic>wt</italic> in a domain-swapped supramolecular array.
520 $a The crystal structure of CAP in complex with αCTD and DNA was solved to a limiting resolution of 3.1Å. The complex provides a structural view of the interactions between CAP-αCTD and αCTD-DNA as well as the importance of DNA bending in transcriptional activation. The structure confirms that the 287 determinant of αCTD interacts with the AR1 loop of CAP and that the 265 determinant of αCTD interacts with DNA minor groove adjacent to the DNA binding site for CAP. Genetic and biochemical experiments alluded to the key amino-acid residues involved CAP-αCTD-DNA interactions and the described crystallographic complex provides a structural rationale for those observations.
520 $a A temperature sensitive (ts) mutant of Trp apo-repressor was solved to a limiting resolution of l.6Å. The crystal structure of the mutant displays an unusual alpha helical bulge occurring in the DNA recognition region of one subunit. The alpha-helical bulge provides a rationale for the repressors inability to function properly at an elevated temperature. Trp <italic>wt </italic> apo-repressor crystallized under the same conditions and does not form this bulge.
520 $a Initial crystal screening of the Trp is mutant lead to the discovery that Trp repressor can form a domain-swapped supramolecular array. Crystallization in &sim;30% isopropyl alcohol produces a structure where a node consisting of four subunits resembles the normal biological homodimer consisting of two intertwined dimers. One helix is unfolded and acts as a bridge connecting neighboring nodes. The biological relevance remains unclear; however, there are potential applications for use in nanotechnology.
590 $a School code: 0190.
650 4 $a Chemistry, Biochemistry. $3 1017722
650 4 $a Biophysics, General. $3 1019105
690 $a 0487
690 $a 0786
710 2 0 $a Rutgers The State University of New Jersey - New Brunswick. $3 1017590
773 0 $t Dissertation Abstracts International $g 64-06B.
790 1 0 $a Berman, Helen M., $e advisor
790 $a 0190
791 $a Ph.D.
792 $a 2003
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3092916