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[[Image:1jyf.jpg|left|200px]]


{{Structure
==Structure of the Dimeric Lac Repressor with an 11-residue C-terminal Deletion.==
|PDB= 1jyf |SIZE=350|CAPTION= <scene name='initialview01'>1jyf</scene>, resolution 3.00&Aring;
<StructureSection load='1jyf' size='340' side='right'caption='[[1jyf]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
<table><tr><td colspan='2'>[[1jyf]] is a 1 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=1JYF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JYF 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]] 3&#8491;</td></tr>
|GENE= LacI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1jyf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jyf OCA], [https://pdbe.org/1jyf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jyf RCSB], [https://www.ebi.ac.uk/pdbsum/1jyf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jyf ProSAT]</span></td></tr>
|RELATEDENTRY=[[1jye|1JYE]]
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jyf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jyf OCA], [http://www.ebi.ac.uk/pdbsum/1jyf PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1jyf RCSB]</span>
== Function ==
}}
[https://www.uniprot.org/uniprot/LACI_ECOLI LACI_ECOLI] Repressor of the lactose operon. Binds allolactose as an inducer.
== 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/jy/1jyf_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=1jyf ConSurf].
<div style="clear:both"></div>


'''Structure of the Dimeric Lac Repressor with an 11-residue C-terminal Deletion.'''
==See Also==
 
*[[Lac repressor|Lac repressor]]
 
__TOC__
==Overview==
</StructureSection>
A single amino acid substitution, K84L, in the Escherichia coli lac repressor produces a protein that has substantially increased stability compared to wild-type. However, despite the increased stability, this altered tetrameric repressor has a tenfold reduced affinity for operator and greatly decreased rate-constants of inducer binding as well as a reduced phenotypic response to inducer in vivo. To understand the dramatic increase in stability and altered functional properties, we have determined the X-ray crystal structures of a dimeric repressor with and without the K84L substitution at resolutions of 1.7 and 3.0 A, respectively. In the wild-type dimer, K84-11, Lys84 forms electrostatic interactions at the monomer-monomer interface and is partially exposed to solvent. In the K84L-11 substituted protein there is reorientation of the N-subdomains, which allows the leucine to become deeply buried at the monomer-monomer interface. This reorientation of the N-subdomains, in turn, results in an alteration of hydrogen bonding, ion pairing, and van der Waals interactions at the monomer-monomer interface. The lysine residue at position 84 appears to exert its key effects by destabilizing the "optimal" conformation of the repressor, effectively loosening the dimer interface and allowing the repressor to adopt the conformations necessary to function as a molecular switch.
 
==About this Structure==
1JYF 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=1JYF OCA].
 
==Reference==
Structure of a variant of lac repressor with increased thermostability and decreased affinity for operator., Bell CE, Barry J, Matthews KS, Lewis M, J Mol Biol. 2001 Oct 12;313(1):99-109. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11601849 11601849]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Barry, J.]]
[[Category: Barry J]]
[[Category: Bell, C E.]]
[[Category: Bell CE]]
[[Category: Lewis, M.]]
[[Category: Lewis M]]
[[Category: Matthews, K S.]]
[[Category: Matthews KS]]
[[Category: gene regulation]]
[[Category: protein dna-binding]]
[[Category: protein stability]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:40:48 2008''

Latest revision as of 10:42, 7 February 2024

Structure of the Dimeric Lac Repressor with an 11-residue C-terminal Deletion.Structure of the Dimeric Lac Repressor with an 11-residue C-terminal Deletion.

Structural highlights

1jyf is a 1 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 3Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

LACI_ECOLI Repressor of the lactose operon. Binds allolactose as an inducer.

Evolutionary Conservation

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

See Also

1jyf, resolution 3.00Å

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