1wlc
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1wlc |SIZE=350|CAPTION= <scene name='initialview01'>1wlc</scene>, resolution 2.0Å | |PDB= 1wlc |SIZE=350|CAPTION= <scene name='initialview01'>1wlc</scene>, resolution 2.0Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC ACID'>MES</scene> | + | |LIGAND= <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1wld|1WLD]], [[1is3|1IS3]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1wlc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wlc OCA], [http://www.ebi.ac.uk/pdbsum/1wlc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1wlc RCSB]</span> | ||
}} | }} | ||
| Line 29: | Line 32: | ||
[[Category: Shionyu-Mitsuyama, C.]] | [[Category: Shionyu-Mitsuyama, C.]] | ||
[[Category: Shirai, T.]] | [[Category: Shirai, T.]] | ||
| - | [[Category: MES]] | ||
[[Category: beta-sandwich]] | [[Category: beta-sandwich]] | ||
[[Category: double-mutant]] | [[Category: double-mutant]] | ||
| Line 35: | Line 37: | ||
[[Category: thermostability]] | [[Category: thermostability]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:37:45 2008'' |
Revision as of 21:37, 30 March 2008
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| , resolution 2.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Related: | 1WLD, 1IS3
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Congerin II Y16S/T88I double mutant
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.
About this Structure
1WLC is a Single protein structure of sequence from Conger myriaster. Full crystallographic information is available from OCA.
Reference
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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