1jyf: Difference between revisions

Revision as of 21:06, 1 July 2008

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File:1jyf.png

Template:STRUCTURE 1jyf

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.

Template:ABSTRACT PUBMED 11601849

About this StructureAbout this Structure

1JYF is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

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:11601849

Page seeded by OCA on Tue Jul 1 21:06:14 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''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.===
-==Overview==
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-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_11601849}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11601849 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_11601849}}
 ==About this Structure==
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 [[Category: Protein dna-binding]]
 [[Category: Protein stability]]
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