1f4m: Difference between revisions

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New page: left|200px<br /><applet load="1f4m" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f4m, resolution 2.25Å" /> '''P3(2) CRYSTAL STRUCT...
 
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[[Image:1f4m.jpg|left|200px]]<br /><applet load="1f4m" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1f4m.jpg|left|200px]]<br /><applet load="1f4m" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1f4m, resolution 2.25&Aring;" />
caption="1f4m, resolution 2.25&Aring;" />
'''P3(2) CRYSTAL STRUCTURE OF ALA2ILE2-6, A VERSION OF ROP WITH A REPACKED HYDROPHOBIC CORE AND A NEW FOLD.'''<br />
'''P3(2) CRYSTAL STRUCTURE OF ALA2ILE2-6, A VERSION OF ROP WITH A REPACKED HYDROPHOBIC CORE AND A NEW FOLD.'''<br />


==Overview==
==Overview==
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.
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.


==About this Structure==
==About this Structure==
1F4M is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1F4M OCA].  
1F4M is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F4M OCA].  


==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Bishop, B.]]
[[Category: Bishop, B.]]
[[Category: Brunger, A.T.]]
[[Category: Brunger, A T.]]
[[Category: Regan, L.]]
[[Category: Regan, L.]]
[[Category: Willis, M.A.]]
[[Category: Willis, M A.]]
[[Category: CA]]
[[Category: CA]]
[[Category: dimer]]
[[Category: dimer]]
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[[Category: transcription regulation]]
[[Category: transcription regulation]]


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