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New page: left|200px<br /><applet load="1lli" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lli, resolution 2.100Å" /> '''THE CRYSTAL STRUCTU...
 
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[[Image:1lli.gif|left|200px]]<br /><applet load="1lli" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1lli, resolution 2.100&Aring;" />
'''THE CRYSTAL STRUCTURE OF A MUTANT PROTEIN WITH ALTERED BUT IMPROVED HYDROPHOBIC CORE PACKING'''<br />


==Overview==
==THE CRYSTAL STRUCTURE OF A MUTANT PROTEIN WITH ALTERED BUT IMPROVED HYDROPHOBIC CORE PACKING==
The dense packing observed in protein interiors appears to be crucial for, stabilizing the native structure--even subtle internal substitutions are, usually destabilizing. Thus, steric complementarity of core residues is, thought to be an important criterion for "inverse folding" predictive, methods, which judge whether a newly determined sequence is consistent, with any known folds. A major problem in the development of useful core, packing evaluation algorithms, however, is that there are occasional, mutations that are predicted to disrupt native packing but that yield an, equally or more stable protein. We have solved the crystal structure of, such a variant of lambda repressor, which, despite having three larger, core substitutions, is more stable than the wild type. The structure, reveals that the protein accommodates the potentially disruptive residues, with shifts in its alpha-helical arrangement. The variant is apparently, more stable because its packing is improved--the core has a higher packing, density and little geometric strain. These rearrangements, however, cause, repositioning of functional residues, which result in reduced DNA binding, activity. By comparing these results with the predictions of two core, packing algorithms, it is clear that the protein possesses a relatively, high degree of main-chain flexibility that must be accounted for in order, to predict the full spectrum of compatible core sequences. This study also, shows how, in protein evolution, a particular set of core residue, identities might be selected not because they provide optimal stability, but because they provide sufficient stability in addition to the precise, structure required for optimal activity.
<StructureSection load='1lli' size='340' side='right'caption='[[1lli]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1lli]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_Lambda Escherichia virus Lambda]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LLI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LLI FirstGlance]. <br>
1LLI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_lambda Enterobacteria phage lambda]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LLI OCA].  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
 
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1lli FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lli OCA], [https://pdbe.org/1lli PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lli RCSB], [https://www.ebi.ac.uk/pdbsum/1lli PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lli ProSAT]</span></td></tr>
==Reference==
</table>
The crystal structure of a mutant protein with altered but improved hydrophobic core packing., Lim WA, Hodel A, Sauer RT, Richards FM, Proc Natl Acad Sci U S A. 1994 Jan 4;91(1):423-7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8278404 8278404]
== Function ==
[[Category: Enterobacteria phage lambda]]
[https://www.uniprot.org/uniprot/RPC1_LAMBD RPC1_LAMBD] Repressor protein CI allows phage lambda to reside inactively in the chromosome of its host bacterium. This lysogenic state is maintained by binding of regulatory protein CI to the OR and OL operators, preventing transcription of proteins necessary for lytic development.
[[Category: Single protein]]
== Evolutionary Conservation ==
[[Category: Hodel, A.]]
[[Image:Consurf_key_small.gif|200px|right]]
[[Category: Lim, W.A.]]
Check<jmol>
[[Category: Richards, F.M.]]
  <jmolCheckbox>
[[Category: Sauer, R.T.]]
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ll/1lli_consurf.spt"</scriptWhenChecked>
[[Category: double helix]]
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
[[Category: protein-dna complex]]
    <text>to colour the structure by Evolutionary Conservation</text>
 
  </jmolCheckbox>
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:39:23 2007''
</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=1lli ConSurf].
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Escherichia virus Lambda]]
[[Category: Large Structures]]
[[Category: Hodel A]]
[[Category: Lim WA]]
[[Category: Richards FM]]
[[Category: Sauer RT]]

Latest revision as of 07:34, 14 February 2024

THE CRYSTAL STRUCTURE OF A MUTANT PROTEIN WITH ALTERED BUT IMPROVED HYDROPHOBIC CORE PACKING

1lli, resolution 2.10Å

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