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1gto

From Proteopedia

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(New page: 200px<br /><applet load="1gto" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gto, resolution 1.82&Aring;" /> '''HIGH RESOLUTION STRU...)
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[[Image:1gto.gif|left|200px]]<br /><applet load="1gto" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1gto, resolution 1.82&Aring;" />
 
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'''HIGH RESOLUTION STRUCTURE OF A HYPERSTABLE HELICAL BUNDLE PROTEIN MUTANT'''<br />
 
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==Overview==
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==HIGH RESOLUTION STRUCTURE OF A HYPERSTABLE HELICAL BUNDLE PROTEIN MUTANT==
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A surface turn position in a four-helix bundle protein, Rop, was selected, to investigate the role of turns in protein structure and stability., Although all twenty amino acids can be substituted at this position to, generate a correctly folded protein, they produce an unusually large range, of thermodynamic stabilities. Moreover, the majority of substitutions give, rise to proteins with enhanced thermal stability compared to that of the, wild type. By introducing the same twenty mutations at this position, but, in a simplified context, we were able to deconvolute intrinsic preferences, from local environmental effects. The intrinsic preferences can be, explained on the basis of preferred backbone dihedral angles, but local, environmental context can significantly modify these effects.
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<StructureSection load='1gto' size='340' side='right'caption='[[1gto]], [[Resolution|resolution]] 1.82&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1gto]] is a 3 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=1GTO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GTO 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]] 1.82&#8491;</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=1gto FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gto OCA], [https://pdbe.org/1gto PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gto RCSB], [https://www.ebi.ac.uk/pdbsum/1gto PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gto 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/gt/1gto_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=1gto 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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1GTO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GTO 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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Amino-acid substitutions in a surface turn modulate protein stability., Predki PF, Agrawal V, Brunger AT, Regan L, Nat Struct Biol. 1996 Jan;3(1):54-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8548455 8548455]
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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: Agrawal, V.]]
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[[Category: Agrawal V]]
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[[Category: Brunger, A.T.]]
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[[Category: Brunger AT]]
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[[Category: Predki, P.]]
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[[Category: Predki P]]
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[[Category: Regan, L.]]
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[[Category: Regan L]]
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[[Category: crystal contacts]]
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[[Category: helix packing]]
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[[Category: transcription regulation]]
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[[Category: turn]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:17:05 2007''
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HIGH RESOLUTION STRUCTURE OF A HYPERSTABLE HELICAL BUNDLE PROTEIN MUTANT

PDB ID 1gto

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