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1f4m
From Proteopedia
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| - | [[Image:1f4m.jpg|left|200px]] | + | [[Image:1f4m.jpg|left|200px]] |
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| - | '''P3(2) CRYSTAL STRUCTURE OF ALA2ILE2-6, A VERSION OF ROP WITH A REPACKED HYDROPHOBIC CORE AND A NEW FOLD.''' | + | {{Structure |
| + | |PDB= 1f4m |SIZE=350|CAPTION= <scene name='initialview01'>1f4m</scene>, resolution 2.25Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''P3(2) CRYSTAL STRUCTURE OF ALA2ILE2-6, A VERSION OF ROP WITH A REPACKED HYDROPHOBIC CORE AND A NEW FOLD.''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1F4M is a [ | + | 1F4M is a [[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=1F4M OCA]. |
==Reference== | ==Reference== | ||
| - | Dramatic structural and thermodynamic consequences of repacking a protein's hydrophobic core., Willis MA, Bishop B, Regan L, Brunger AT, Structure. 2000 Dec 15;8(12):1319-28. PMID:[http:// | + | Dramatic structural and thermodynamic consequences of repacking a protein's hydrophobic core., Willis MA, Bishop B, Regan L, Brunger AT, Structure. 2000 Dec 15;8(12):1319-28. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11188696 11188696] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transcription regulation]] | [[Category: transcription regulation]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:04:21 2008'' |
Revision as of 09:04, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
P3(2) CRYSTAL STRUCTURE OF ALA2ILE2-6, A VERSION OF ROP WITH A REPACKED HYDROPHOBIC CORE AND A NEW FOLD.
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.
About this Structure
1F4M is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Dramatic structural and thermodynamic consequences of repacking a protein's hydrophobic core., Willis MA, Bishop B, Regan L, Brunger AT, Structure. 2000 Dec 15;8(12):1319-28. PMID:11188696
Page seeded by OCA on Thu Mar 20 11:04:21 2008
