1f4n: Difference between revisions

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[[Image:1f4n.jpg|left|200px]]
{{Seed}}
[[Image:1f4n.png|left|200px]]


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{{STRUCTURE_1f4n|  PDB=1f4n  |  SCENE=  }}  
{{STRUCTURE_1f4n|  PDB=1f4n  |  SCENE=  }}  


'''C2 CRYSTAL STRUCTURE OF ALA2ILE2-6, A VERSION OF ROP WITH A REPACKED HYDROPHOBIC CORE AND A NEW FOLD.'''
===C2 CRYSTAL STRUCTURE OF ALA2ILE2-6, A VERSION OF ROP WITH A REPACKED HYDROPHOBIC CORE AND A NEW FOLD.===




==Overview==
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BACKGROUND: Rop is an RNA binding, dimeric, four-helix bundle protein with a well-defined, regular hydrophobic core ideally suited for redesign studies. A family of Rop variants in which the hydrophobic core was systematically redesigned has previously been created and characterized. RESULTS: We present a structural and thermodynamic analysis of Ala2Ile2-6, a variant of Rop with an extensively redesigned hydrophobic core. The structure of Ala2Ile2-6 reveals a completely new fold formed by a conformational "flip" of the two protomers around the dimeric interface. The free-energy profile of Ala2Ile2-6 is also very different from that of wild-type Rop. Ala2Ile2-6 has a higher melting temperature than Rop, but undergoes a slightly smaller free-energy change on unfolding. CONCLUSIONS: The structure of Ala2Ile2-6, along with molecular modeling results, demonstrate the importance of tight packing of core residues and the adoption of favorable core side chain rotamer values in determining helix-helix interactions in the four-helix bundle fold. Structural disorder at the N and C termini of Ala2Ile2-6 provides a basis for the large differences in the enthalpy and entropy of Ala2Ile2-6 folding compared with wildtype Rop.
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{{ABSTRACT_PUBMED_11188696}}


==About this Structure==
==About this Structure==
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[[Category: Thermodynamic stability]]
[[Category: Thermodynamic stability]]
[[Category: Transcription regulation]]
[[Category: Transcription regulation]]
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