1rpr: Difference between revisions

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[[Image:1rpr.jpg|left|200px]]<br /><applet load="1rpr" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1rpr.jpg|left|200px]]<br /><applet load="1rpr" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1rpr" />

'''THE STRUCTURE OF COLE1 ROP IN SOLUTION'''<br />

==Overview==

The structure of the ColE1 repressor of primer (rop) protein in solution, was determined from the proton nuclear magnetic resonance data by a, combined use of distance geometry and restrained molecular dynamics, calculations. A set of structures was determined with low internal energy, and virtually no violations of the experimental distance restraints. Rop, forms homodimers: Two helical hairpins are arranged as an antiparallel, four helix bundle with a left-handed rope-like twist of the helix axes and, with left-handed bundle topology. The very compact packing of the side, chains in the helix interfaces of the rop coiled-coil structure may well, account for its high stability. Overall, the solution structure is highly, similar to the recently determined X-ray structure (Banner, D.W., Kokkinidis, M. and Tsernoglou, D. (1987) J. Mol. Biol., 196, 657-675), although there are minor differences in regions where packing forces, appear to influence the crystal structure.

The structure of the ColE1 repressor of primer (rop) protein in solution was determined from the proton nuclear magnetic resonance data by a combined use of distance geometry and restrained molecular dynamics calculations. A set of structures was determined with low internal energy and virtually no violations of the experimental distance restraints. Rop forms homodimers: Two helical hairpins are arranged as an antiparallel four helix bundle with a left-handed rope-like twist of the helix axes and with left-handed bundle topology. The very compact packing of the side chains in the helix interfaces of the rop coiled-coil structure may well account for its high stability. Overall, the solution structure is highly similar to the recently determined X-ray structure (Banner, D.W., Kokkinidis, M. and Tsernoglou, D. (1987) J. Mol. Biol., 196, 657-675), although there are minor differences in regions where packing forces appear to influence the crystal structure.

==About this Structure==

1RPR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1RPR OCA].

1RPR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RPR OCA].

==Reference==

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[[Category: transcription regulation]]

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@@ Line 1: / Line 1: @@
-[[Image:1rpr.jpg|left|200px]]<br /><applet load="1rpr" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1rpr.jpg|left|200px]]<br /><applet load="1rpr" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1rpr" />
 '''THE STRUCTURE OF COLE1 ROP IN SOLUTION'''<br />
 ==Overview==
-The structure of the ColE1 repressor of primer (rop) protein in solution, was determined from the proton nuclear magnetic resonance data by a, combined use of distance geometry and restrained molecular dynamics, calculations. A set of structures was determined with low internal energy, and virtually no violations of the experimental distance restraints. Rop, forms homodimers: Two helical hairpins are arranged as an antiparallel, four helix bundle with a left-handed rope-like twist of the helix axes and, with left-handed bundle topology. The very compact packing of the side, chains in the helix interfaces of the rop coiled-coil structure may well, account for its high stability. Overall, the solution structure is highly, similar to the recently determined X-ray structure (Banner, D.W., Kokkinidis, M. and Tsernoglou, D. (1987) J. Mol. Biol., 196, 657-675), although there are minor differences in regions where packing forces, appear to influence the crystal structure.
+The structure of the ColE1 repressor of primer (rop) protein in solution was determined from the proton nuclear magnetic resonance data by a combined use of distance geometry and restrained molecular dynamics calculations. A set of structures was determined with low internal energy and virtually no violations of the experimental distance restraints. Rop forms homodimers: Two helical hairpins are arranged as an antiparallel four helix bundle with a left-handed rope-like twist of the helix axes and with left-handed bundle topology. The very compact packing of the side chains in the helix interfaces of the rop coiled-coil structure may well account for its high stability. Overall, the solution structure is highly similar to the recently determined X-ray structure (Banner, D.W., Kokkinidis, M. and Tsernoglou, D. (1987) J. Mol. Biol., 196, 657-675), although there are minor differences in regions where packing forces appear to influence the crystal structure.
 ==About this Structure==
-RPR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RPR OCA].
+RPR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RPR OCA].
 ==Reference==
@@ Line 20: / Line 20: @@
 [[Category: transcription regulation]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:46:48 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:53:17 2008''