1rpe
From Proteopedia
(New page: 200px<br /> <applet load="1rpe" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rpe, resolution 2.500Å" /> '''THE PHAGE 434 OR2/...) |
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| - | [[Image:1rpe.gif|left|200px]]<br /> | + | [[Image:1rpe.gif|left|200px]]<br /><applet load="1rpe" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1rpe" size=" | + | |
caption="1rpe, resolution 2.500Å" /> | caption="1rpe, resolution 2.500Å" /> | ||
'''THE PHAGE 434 OR2/R1-69 COMPLEX AT 2.5 ANGSTROMS RESOLUTION'''<br /> | '''THE PHAGE 434 OR2/R1-69 COMPLEX AT 2.5 ANGSTROMS RESOLUTION'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of the DNA-binding domain of bacteriophage 434 | + | The crystal structure of the DNA-binding domain of bacteriophage 434 repressor (R1-69) in complex with a 20 base-pair DNA fragment has been determined to 2.5 A resolution. The DNA fragment contains the sequence of the OR2 operator site, which differs from the previously studied OR1 site at three of the variable six central base-pairs. Comparison of the two structures shows that the overall bent conformation of the DNA backbone as well as the pattern of DNA-protein interactions seen in the OR1/R1-69 complex are maintained in the OR2 complex. However, the conformations of the DNA base-pairs are different in the two structures. In particular, the central base-pairs of OR2/R1-69 structure are more co-planar than in OR1/R1-69, and there are no cross-strand "bifurcated" hydrogen bonds. These results show that binding of the protein causes operator DNA to adopt a particular, well-defined backbone conformation, and they reinforce the notion that the energetic cost of achieving this conformation, most likely different for different sequences, can determine, at least in part, the relative affinity of the repressor for different operator sites. |
==About this Structure== | ==About this Structure== | ||
| - | 1RPE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_434 Bacteriophage 434]. Full crystallographic information is available from [http:// | + | 1RPE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_434 Bacteriophage 434]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RPE OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Bacteriophage 434]] | [[Category: Bacteriophage 434]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Harrison, S | + | [[Category: Harrison, S C.]] |
| - | [[Category: Shimon, L | + | [[Category: Shimon, L J.W.]] |
[[Category: double helix]] | [[Category: double helix]] | ||
[[Category: protein-dna complex]] | [[Category: protein-dna complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:53:11 2008'' |
Revision as of 12:53, 21 February 2008
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THE PHAGE 434 OR2/R1-69 COMPLEX AT 2.5 ANGSTROMS RESOLUTION
Overview
The crystal structure of the DNA-binding domain of bacteriophage 434 repressor (R1-69) in complex with a 20 base-pair DNA fragment has been determined to 2.5 A resolution. The DNA fragment contains the sequence of the OR2 operator site, which differs from the previously studied OR1 site at three of the variable six central base-pairs. Comparison of the two structures shows that the overall bent conformation of the DNA backbone as well as the pattern of DNA-protein interactions seen in the OR1/R1-69 complex are maintained in the OR2 complex. However, the conformations of the DNA base-pairs are different in the two structures. In particular, the central base-pairs of OR2/R1-69 structure are more co-planar than in OR1/R1-69, and there are no cross-strand "bifurcated" hydrogen bonds. These results show that binding of the protein causes operator DNA to adopt a particular, well-defined backbone conformation, and they reinforce the notion that the energetic cost of achieving this conformation, most likely different for different sequences, can determine, at least in part, the relative affinity of the repressor for different operator sites.
About this Structure
1RPE is a Single protein structure of sequence from Bacteriophage 434. Full crystallographic information is available from OCA.
Reference
The phage 434 OR2/R1-69 complex at 2.5 A resolution., Shimon LJ, Harrison SC, J Mol Biol. 1993 Aug 5;232(3):826-38. PMID:8355273
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