1f4m
From Proteopedia
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|PDB= 1f4m |SIZE=350|CAPTION= <scene name='initialview01'>1f4m</scene>, resolution 2.25Å | |PDB= 1f4m |SIZE=350|CAPTION= <scene name='initialview01'>1f4m</scene>, resolution 2.25Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1f4n|1F4N]], [[1rop|1ROP]], [[1gto|1GTO]], [[1nkd|1NKD]], [[1rpo|1RPO]], [[1b6q|1B6Q]], [[1rpr|1RPR]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1f4m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f4m OCA], [http://www.ebi.ac.uk/pdbsum/1f4m PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1f4m RCSB]</span> | ||
}} | }} | ||
| Line 26: | Line 29: | ||
[[Category: Regan, L.]] | [[Category: Regan, L.]] | ||
[[Category: Willis, M A.]] | [[Category: Willis, M A.]] | ||
| - | [[Category: CA]] | ||
[[Category: dimer]] | [[Category: dimer]] | ||
[[Category: helix-turn-helix]] | [[Category: helix-turn-helix]] | ||
| Line 35: | Line 37: | ||
[[Category: transcription regulation]] | [[Category: transcription regulation]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:15:43 2008'' |
Revision as of 17:15, 30 March 2008
| |||||||
| , resolution 2.25Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Related: | 1F4N, 1ROP, 1GTO, 1NKD, 1RPO, 1B6Q, 1RPR
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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
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