1wlc: Difference between revisions

Revision as of 16:45, 21 February 2008

Congerin II Y16S/T88I double mutant

OverviewOverview

The thermostability of the conger eel galectin, congerin II, was improved by in vitro evolutionary protein engineering. Two rounds of random PCR mutagenesis and selection experiments increased the congerin II thermostability to a level comparative to its naturally thermostable isoform, congerin I. The crystal structures of the most thermostable double mutant, Y16S/T88I, and the related single mutants, Y16S and T88I, were determined at 2.0 angstroms, 1.8 angstroms, and 1.6 angstroms resolution, respectively. The exclusion of two interior water molecules by the Thr88Ile mutation, and the relief of adjacent conformational stress by the Tyr16Ser mutation were the major contributions to the thermostability. These features in the congerin II mutants are similar to those observed in congerin I. The natural evolution of congerin genes, with the K(A)/K(S) ratio of 2.6, was accelerated under natural selection pressures. The thermostabilizing selection pressure artificially applied to congerin II mimicked the implied natural pressure on congerin I. The results showed that the artificial pressure made congerin II partially reproduce the natural evolution of congerin I.

About this StructureAbout this Structure

1WLC is a Single protein structure of sequence from Conger myriaster with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

In vitro evolutionary thermostabilization of congerin II: a limited reproduction of natural protein evolution by artificial selection pressure., Shionyu-Mitsuyama C, Ito Y, Konno A, Miwa Y, Ogawa T, Muramoto K, Shirai T, J Mol Biol. 2005 Mar 25;347(2):385-97. Epub 2005 Jan 27. PMID:15740748

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OCA

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-[[Image:1wlc.gif|left|200px]]<br /><applet load="1wlc" size="450" color="white" frame="true" align="right" spinBox="true"
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 caption="1wlc, resolution 2.0&Aring;" />
 '''Congerin II Y16S/T88I double mutant'''<br />
 ==Overview==
-The thermostability of the conger eel galectin, congerin II, was improved, by in vitro evolutionary protein engineering. Two rounds of random PCR, mutagenesis and selection experiments increased the congerin II, thermostability to a level comparative to its naturally thermostable, isoform, congerin I. The crystal structures of the most thermostable, double mutant, Y16S/T88I, and the related single mutants, Y16S and T88I, were determined at 2.0 angstroms, 1.8 angstroms, and 1.6 angstroms, resolution, respectively. The exclusion of two interior water molecules by, the Thr88Ile mutation, and the relief of adjacent conformational stress by, the Tyr16Ser mutation were the major contributions to the thermostability., These features in the congerin II mutants are similar to those observed in, congerin I. The natural evolution of congerin genes, with the K(A)/K(S), ratio of 2.6, was accelerated under natural selection pressures. The, thermostabilizing selection pressure artificially applied to congerin II, mimicked the implied natural pressure on congerin I. The results showed, that the artificial pressure made congerin II partially reproduce the, natural evolution of congerin I.
+The thermostability of the conger eel galectin, congerin II, was improved by in vitro evolutionary protein engineering. Two rounds of random PCR mutagenesis and selection experiments increased the congerin II thermostability to a level comparative to its naturally thermostable isoform, congerin I. The crystal structures of the most thermostable double mutant, Y16S/T88I, and the related single mutants, Y16S and T88I, were determined at 2.0 angstroms, 1.8 angstroms, and 1.6 angstroms resolution, respectively. The exclusion of two interior water molecules by the Thr88Ile mutation, and the relief of adjacent conformational stress by the Tyr16Ser mutation were the major contributions to the thermostability. These features in the congerin II mutants are similar to those observed in congerin I. The natural evolution of congerin genes, with the K(A)/K(S) ratio of 2.6, was accelerated under natural selection pressures. The thermostabilizing selection pressure artificially applied to congerin II mimicked the implied natural pressure on congerin I. The results showed that the artificial pressure made congerin II partially reproduce the natural evolution of congerin I.
 ==About this Structure==
-WLC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Conger_myriaster Conger myriaster] with MES as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1WLC OCA].
+WLC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Conger_myriaster Conger myriaster] with <scene name='pdbligand=MES:'>MES</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WLC OCA].
 ==Reference==
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 [[Category: thermostability]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 05:30:21 2007''
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