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Determination of the crystal structu...

Struble, Evi Budo.

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Determination of the crystal structure of bacteriophage lambda replication initiator N-terminal fragment.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Determination of the crystal structure of bacteriophage lambda replication initiator N-terminal fragment./
作者:	Struble, Evi Budo.
面頁冊數:	137 p.
附註:	Source: Dissertation Abstracts International, Volume: 65-12, Section: B, page: 6241.
Contained By:	Dissertation Abstracts International65-12B.
標題:	Biophysics, General. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3155688
ISBN:	9780496164943

Determination of the crystal structure of bacteriophage lambda replication initiator N-terminal fragment.
Struble, Evi Budo.

Determination of the crystal structure of bacteriophage lambda replication initiator N-terminal fragment. - 137 p.

Source: Dissertation Abstracts International, Volume: 65-12, Section: B, page: 6241.

Thesis (Ph.D.)--The Johns Hopkins University, 2005.

Bacteriophage lambda replication initiator, known as lambda O protein, is one of the two replication proteins encoded by the bacteriophage's own genome. Its role in initiating bacteriophage DNA replication has been firmly established and several models have been constructed to describe its involvement in DNA bending at the lambdaori region.

ISBN: 9780496164943Subjects--Topical Terms:

1019105
Biophysics, General.

Determination of the crystal structure of bacteriophage lambda replication initiator N-terminal fragment.
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245 1 0 $a Determination of the crystal structure of bacteriophage lambda replication initiator N-terminal fragment.
300 $a 137 p.
500 $a Source: Dissertation Abstracts International, Volume: 65-12, Section: B, page: 6241.
500 $a Adviser: Eaton Lattman.
502 $a Thesis (Ph.D.)--The Johns Hopkins University, 2005.
520 $a Bacteriophage lambda replication initiator, known as lambda O protein, is one of the two replication proteins encoded by the bacteriophage's own genome. Its role in initiating bacteriophage DNA replication has been firmly established and several models have been constructed to describe its involvement in DNA bending at the lambdaori region.
520 $a Solution studies of lambda O protein fragment 19-139 helped to determine its crystallization conditions. Although crystals obtained for protein/DNA complexes did not diffract to high resolution, the crystals consisting of lambda O protein N-terminal fragment diffracted to 2.5 A. These crystals belonged to space group p21212. There are two lambda O dimers in the asymmetric unit, related to each other by a two-fold non-crystallographic symmetry operator parallel to the z-axis.
520 $a The crystal structure of the fragment 19-139 of lambda O protein has been solved to 2.5 A resolution by using anomalous dispersion of selenium atoms. Residues 19-29 and 118-139 are disordered and not modeled in the solved structure. The structure displays the winged-helix motif, with one additional beta-strand and one alpha-helix at the N-terminus. These two elements, in combination with the first alpha-helix of the winged-helix motif are involved in dimerization contacts between two lambda O monomers.
520 $a Despite very low homology at the amino-acid sequence level (11% for the structurally aligned regions), the DNA-binding region of lambda O displays great similarity to the Catabolite Activator Protein (CAP) DNA-binding domain. This structural homology, in combination with genetic data, indicates a DNA-binding mode for lambda O protein that is similar to the one present in CAP.
520 $a The dimerization domain of lambda O protein shows structural similarity with another prokaryotic replication initiator, RepE.
520 $a The structural homologies unveiled by the new structure of lambda O N-terminal fragment could have functional and evolutionary implications that need to be further explored.
590 $a School code: 0098.
650 4 $a Biophysics, General. $3 1019105
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791 $a Ph.D.
792 $a 2005
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