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[[Image:1gto.gif|left|200px]]


{{Structure
==HIGH RESOLUTION STRUCTURE OF A HYPERSTABLE HELICAL BUNDLE PROTEIN MUTANT==
|PDB= 1gto |SIZE=350|CAPTION= <scene name='initialview01'>1gto</scene>, resolution 1.82&Aring;
<StructureSection load='1gto' size='340' side='right'caption='[[1gto]], [[Resolution|resolution]] 1.82&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND=  
<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>
|ACTIVITY=  
</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>
|GENE=  
<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>
}}
</table>
== Function ==
[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.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gt/1gto_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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].
<div style="clear:both"></div>


'''HIGH RESOLUTION STRUCTURE OF A HYPERSTABLE HELICAL BUNDLE PROTEIN MUTANT'''
==See Also==
 
*[[Rop protein|Rop protein]]
 
__TOC__
==Overview==
</StructureSection>
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.
 
==About this Structure==
1GTO 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=1GTO OCA].
 
==Reference==
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://www.ncbi.nlm.nih.gov/pubmed/8548455 8548455]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Agrawal, V.]]
[[Category: Agrawal V]]
[[Category: Brunger, A T.]]
[[Category: Brunger AT]]
[[Category: Predki, P.]]
[[Category: Predki P]]
[[Category: Regan, L.]]
[[Category: Regan L]]
[[Category: crystal contact]]
[[Category: helix packing]]
[[Category: transcription regulation]]
[[Category: turn]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:27:44 2008''

Latest revision as of 10:26, 7 February 2024

HIGH RESOLUTION STRUCTURE OF A HYPERSTABLE HELICAL BUNDLE PROTEIN MUTANTHIGH RESOLUTION STRUCTURE OF A HYPERSTABLE HELICAL BUNDLE PROTEIN MUTANT

Structural highlights

1gto is a 3 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.82Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1gto, resolution 1.82Å

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