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A structural genomics analysis of hi...

Cheung, Jonah.

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A structural genomics analysis of histidine kinase sensor domains.

Record Type:	Electronic resources : Monograph/item
Title/Author:	A structural genomics analysis of histidine kinase sensor domains./
Author:	Cheung, Jonah.
Description:	178 p.
Notes:	Source: Dissertation Abstracts International, Volume: 66-05, Section: B, page: 2565.
Contained By:	Dissertation Abstracts International66-05B.
Subject:	Chemistry, Biochemistry. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3174764
ISBN:	0542130793

A structural genomics analysis of histidine kinase sensor domains.
Cheung, Jonah.

A structural genomics analysis of histidine kinase sensor domains. - 178 p.

Source: Dissertation Abstracts International, Volume: 66-05, Section: B, page: 2565.

Thesis (Ph.D.)--Columbia University, 2005.

Histidine kinase sensors are a part of a two-component system of protein signaling in prokaryotes and lower eukaryotes that relay an external environmental signal to an adaptive internal cellular response. Signal transduction occurs via phosphotransfer between a sensor protein and a response regulator which interact in tandem. The sensor is usually a transmembrane protein that contains a conserved cytoplasmic histidine kinase transmitter domain and a modular periplasmic sensor domain. The response regulator is cytoplasmic protein that contains a receiver domain that interacts with the histidine kinase, and an output domain that interacts with regulators of transcription or chemotaxis. My work focuses on the X-ray structure determination of a variety of bacterial sensor domains, based on a structural genomics analysis of the entire sensor domain family. Structures of the NarX, DcuS, LisK, and DctB sensor domains have been solved to atomic resolution, some in both ligand-bound and ligand-free states. Two distinct structural folds have been revealed---all-alpha helical and mixed alpha-beta. An analysis of the structures reveals a possible mechanism of transmembrane signaling in histidine kinase sensors as a sliding-piston motion between transmembrane helices. Although there is great diversity in ligand binding, there appears to be a small number of distinct sensor domain folds for which structural representatives of two have been solved. A final synthesis of the structural information with a comprehensive bio-informatics analysis of all histidine kinase sensor domain sequences allows fold prediction for over 400 sensor domains, in a step towards mapping the entire structural landscape of this protein family.

ISBN: 0542130793Subjects--Topical Terms:

1017722
Chemistry, Biochemistry.

A structural genomics analysis of histidine kinase sensor domains.
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040 $a UnM $c UnM
100 1 $a Cheung, Jonah. $3 1903459
245 1 2 $a A structural genomics analysis of histidine kinase sensor domains.
300 $a 178 p.
500 $a Source: Dissertation Abstracts International, Volume: 66-05, Section: B, page: 2565.
500 $a Adviser: Wayne Hendrickson.
502 $a Thesis (Ph.D.)--Columbia University, 2005.
520 $a Histidine kinase sensors are a part of a two-component system of protein signaling in prokaryotes and lower eukaryotes that relay an external environmental signal to an adaptive internal cellular response. Signal transduction occurs via phosphotransfer between a sensor protein and a response regulator which interact in tandem. The sensor is usually a transmembrane protein that contains a conserved cytoplasmic histidine kinase transmitter domain and a modular periplasmic sensor domain. The response regulator is cytoplasmic protein that contains a receiver domain that interacts with the histidine kinase, and an output domain that interacts with regulators of transcription or chemotaxis. My work focuses on the X-ray structure determination of a variety of bacterial sensor domains, based on a structural genomics analysis of the entire sensor domain family. Structures of the NarX, DcuS, LisK, and DctB sensor domains have been solved to atomic resolution, some in both ligand-bound and ligand-free states. Two distinct structural folds have been revealed---all-alpha helical and mixed alpha-beta. An analysis of the structures reveals a possible mechanism of transmembrane signaling in histidine kinase sensors as a sliding-piston motion between transmembrane helices. Although there is great diversity in ligand binding, there appears to be a small number of distinct sensor domain folds for which structural representatives of two have been solved. A final synthesis of the structural information with a comprehensive bio-informatics analysis of all histidine kinase sensor domain sequences allows fold prediction for over 400 sensor domains, in a step towards mapping the entire structural landscape of this protein family.
590 $a School code: 0054.
650 4 $a Chemistry, Biochemistry. $3 1017722
650 4 $a Physics, Molecular. $3 1018648
690 $a 0487
690 $a 0609
710 2 0 $a Columbia University. $3 571054
773 0 $t Dissertation Abstracts International $g 66-05B.
790 1 0 $a Hendrickson, Wayne, $e advisor
790 $a 0054
791 $a Ph.D.
792 $a 2005
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3174764