1rpr
From Proteopedia
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'''THE STRUCTURE OF COLE1 ROP IN SOLUTION''' | '''THE STRUCTURE OF COLE1 ROP IN SOLUTION''' | ||
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[[Category: Roesch, P.]] | [[Category: Roesch, P.]] | ||
[[Category: Sander, C.]] | [[Category: Sander, C.]] | ||
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Revision as of 04:46, 3 May 2008
THE STRUCTURE OF COLE1 ROP IN SOLUTION
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.
About this Structure
1RPR is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
The structure of ColE1 rop in solution., Eberle W, Pastore A, Sander C, Rosch P, J Biomol NMR. 1991 May;1(1):71-82. PMID:1841691 Page seeded by OCA on Sat May 3 07:46:02 2008
