1f4m

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(New page: 200px<br /><applet load="1f4m" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f4m, resolution 2.25&Aring;" /> '''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"
 
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caption="1f4m, resolution 2.25&Aring;" />
 
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'''P3(2) CRYSTAL STRUCTURE OF ALA2ILE2-6, A VERSION OF ROP WITH A REPACKED HYDROPHOBIC CORE AND A NEW FOLD.'''<br />
 
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==Overview==
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==P3(2) CRYSTAL STRUCTURE OF ALA2ILE2-6, A VERSION OF ROP WITH A REPACKED HYDROPHOBIC CORE AND A NEW FOLD.==
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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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<StructureSection load='1f4m' size='340' side='right'caption='[[1f4m]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1f4m]] is a 6 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F4M FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1f4m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f4m OCA], [https://pdbe.org/1f4m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f4m RCSB], [https://www.ebi.ac.uk/pdbsum/1f4m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f4m ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ROP_ECOLX ROP_ECOLX] Regulates plasmid DNA replication by modulating the initiation of transcription of the primer RNA precursor. Processing of the precursor of the primer, RNAII, is inhibited by hydrogen bonding of RNAII to its complementary sequence in RNAI. ROP increases the affinity of RNAI for RNAII and thus decreases the rate of replication initiation events.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f4/1f4m_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1f4m ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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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].
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*[[Rop protein|Rop protein]]
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__TOC__
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==Reference==
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</StructureSection>
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=11188696 11188696]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Bishop, B.]]
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[[Category: Bishop B]]
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[[Category: Brunger, A.T.]]
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[[Category: Brunger AT]]
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[[Category: Regan, L.]]
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[[Category: Regan L]]
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[[Category: Willis, M.A.]]
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[[Category: Willis MA]]
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[[Category: CA]]
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[[Category: dimer]]
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[[Category: helix-turn-helix]]
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[[Category: homodimer]]
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[[Category: hydrophobic core packing]]
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[[Category: rop]]
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[[Category: thermodynamic stability]]
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[[Category: transcription regulation]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:36:46 2007''
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Current revision

P3(2) CRYSTAL STRUCTURE OF ALA2ILE2-6, A VERSION OF ROP WITH A REPACKED HYDROPHOBIC CORE AND A NEW FOLD.

PDB ID 1f4m

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