1kmt
From Proteopedia
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| - | [[Image:1kmt.gif|left|200px]] | + | [[Image:1kmt.gif|left|200px]] |
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| - | '''Crystal structure of RhoGDI Glu(154,155)Ala mutant''' | + | {{Structure |
| + | |PDB= 1kmt |SIZE=350|CAPTION= <scene name='initialview01'>1kmt</scene>, resolution 1.30Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''Crystal structure of RhoGDI Glu(154,155)Ala mutant''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1KMT is a [ | + | 1KMT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KMT OCA]. |
==Reference== | ==Reference== | ||
| - | The impact of Glu-->Ala and Glu-->Asp mutations on the crystallization properties of RhoGDI: the structure of RhoGDI at 1.3 A resolution., Mateja A, Devedjiev Y, Krowarsch D, Longenecker K, Dauter Z, Otlewski J, Derewenda ZS, Acta Crystallogr D Biol Crystallogr. 2002 Dec;58(Pt 12):1983-91. Epub 2002, Nov 23. PMID:[http:// | + | The impact of Glu-->Ala and Glu-->Asp mutations on the crystallization properties of RhoGDI: the structure of RhoGDI at 1.3 A resolution., Mateja A, Devedjiev Y, Krowarsch D, Longenecker K, Dauter Z, Otlewski J, Derewenda ZS, Acta Crystallogr D Biol Crystallogr. 2002 Dec;58(Pt 12):1983-91. Epub 2002, Nov 23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12454455 12454455] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: isoprenyl-binding]] | [[Category: isoprenyl-binding]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:19:31 2008'' |
Revision as of 10:19, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of RhoGDI Glu(154,155)Ala mutant
Overview
It is hypothesized that surface residues with high conformational entropy, specifically lysines and glutamates, impede protein crystallization. In a previous study using a model system of Rho-specific guanine nucleotide dissociation inhibitor (RhoGDI), it was shown that mutating Lys residues to Ala results in enhanced crystallizability, particularly when clusters of lysines are targeted. It was also shown that one of these mutants formed crystals that yielded diffraction to 2.0 A, a significant improvement on the wild-type protein crystals. In the current paper, an analysis of the impact of surface mutations replacing Glu residues with Ala or Asp on the stability and crystallization properties of RhoGDI is presented. The Glu-->Ala (Asp) mutants are generally more likely to produce crystals of the protein than the wild-type and in one case the resulting crystals yielded a diffraction pattern to 1.2 A resolution. This occurs in spite of the fact that mutating surface Glu residues almost invariably affects the protein's stability, as illustrated by the reduced deltaG between folded and unfolded forms measured by isothermal equilibrium denaturation. The present study strongly supports the notion that rational surface mutagenesis can be an effective tool in overcoming problems stemming from the protein's recalcitrance to crystallization and may also yield dramatic improvements in crystal quality.
About this Structure
1KMT is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The impact of Glu-->Ala and Glu-->Asp mutations on the crystallization properties of RhoGDI: the structure of RhoGDI at 1.3 A resolution., Mateja A, Devedjiev Y, Krowarsch D, Longenecker K, Dauter Z, Otlewski J, Derewenda ZS, Acta Crystallogr D Biol Crystallogr. 2002 Dec;58(Pt 12):1983-91. Epub 2002, Nov 23. PMID:12454455
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