2f47: Difference between revisions

Revision as of 03:20, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2f47.png

Template:STRUCTURE 2f47

Xray crystal structure of T4 lysozyme mutant L20/R63A liganded to methylguanidiniumXray crystal structure of T4 lysozyme mutant L20/R63A liganded to methylguanidinium

Template:ABSTRACT PUBMED 16600969

About this StructureAbout this Structure

2F47 is a Single protein structure of sequence from Enterobacteria phage t4. Full crystallographic information is available from OCA.

ReferenceReference

Guanidinium derivatives bind preferentially and trigger long-distance conformational changes in an engineered T4 lysozyme., Yousef MS, Bischoff N, Dyer CM, Baase WA, Matthews BW, Protein Sci. 2006 Apr;15(4):853-61. PMID:16600969

Use of sequence duplication to engineer a ligand-triggered, long-distance molecular switch in T4 lysozyme., Yousef MS, Baase WA, Matthews BW, Proc Natl Acad Sci U S A. 2004 Aug 10;101(32):11583-6. Epub 2004 Jul 30. PMID:15286283

Structural characterization of an engineered tandem repeat contrasts the importance of context and sequence in protein folding., Sagermann M, Baase WA, Matthews BW, Proc Natl Acad Sci U S A. 1999 May 25;96(11):6078-83. PMID:10339544

Long-distance conformational changes in a protein engineered by modulated sequence duplication., Sagermann M, Gay L, Matthews BW, Proc Natl Acad Sci U S A. 2003 Aug 5;100(16):9191-5. Epub 2003 Jul 17. PMID:12869697

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OCA

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 {{STRUCTURE_2f47|  PDB=2f47  |  SCENE=  }}
-'''Xray crystal structure of T4 lysozyme mutant L20/R63A liganded to methylguanidinium'''
+===Xray crystal structure of T4 lysozyme mutant L20/R63A liganded to methylguanidinium===
-==Overview==
+<!--
-The binding of guanidinium ion has been shown to promote a large-scale translation of a tandemly duplicated helix in an engineered mutant of T4 lysozyme. The guanidinium ion acts as a surrogate for the guanidino group of an arginine side chain. Here we determine whether methyl- and ethylguanidinium provide better mimics. The results show that addition of the hydrophobic moieties to the ligand enhances the binding affinity concomitant with reduction in ligand solubility. Crystallographic analysis confirms that binding of the alternative ligands to the engineered site still drives the large-scale conformational change. Thermal analysis and NMR data show, in comparison to guanidinium, an increase in protein stability and in ligand affinity. This is presumably due to the successive increase in hydrophobicity in going from guanidinium to ethylguanidinium. A fluorescence-based optical method was developed to sense the ligand-triggered helix translation in solution. The results are a first step in the de novo design of a molecular switch that is not related to the normal function of the protein.
+The line below this paragraph, {{ABSTRACT_PUBMED_16600969}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16600969 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16600969}}
 ==About this Structure==
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 ==Reference==
 Guanidinium derivatives bind preferentially and trigger long-distance conformational changes in an engineered T4 lysozyme., Yousef MS, Bischoff N, Dyer CM, Baase WA, Matthews BW, Protein Sci. 2006 Apr;15(4):853-61. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16600969 16600969]
+Use of sequence duplication to engineer a ligand-triggered, long-distance molecular switch in T4 lysozyme., Yousef MS, Baase WA, Matthews BW, Proc Natl Acad Sci U S A. 2004 Aug 10;101(32):11583-6. Epub 2004 Jul 30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15286283 15286283]
+Structural characterization of an engineered tandem repeat contrasts the importance of context and sequence in protein folding., Sagermann M, Baase WA, Matthews BW, Proc Natl Acad Sci U S A. 1999 May 25;96(11):6078-83. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10339544 10339544]
+Long-distance conformational changes in a protein engineered by modulated sequence duplication., Sagermann M, Gay L, Matthews BW, Proc Natl Acad Sci U S A. 2003 Aug 5;100(16):9191-5. Epub 2003 Jul 17. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12869697 12869697]
 [[Category: Enterobacteria phage t4]]
 [[Category: Lysozyme]]
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 [[Category: Protein engineering]]
 [[Category: T4 lysozyme]]
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