1qvy
From Proteopedia
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| - | [[Image:1qvy.jpg|left|200px]] | + | [[Image:1qvy.jpg|left|200px]] |
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| - | '''Crystal structure of RhoGDI K(199,200)R double mutant''' | + | {{Structure |
| + | |PDB= 1qvy |SIZE=350|CAPTION= <scene name='initialview01'>1qvy</scene>, resolution 1.60Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''Crystal structure of RhoGDI K(199,200)R double mutant''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1QVY is a [ | + | 1QVY 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=1QVY OCA]. |
==Reference== | ==Reference== | ||
| - | The impact of Lys-->Arg surface mutations on the crystallization of the globular domain of RhoGDI., Czepas J, Devedjiev Y, Krowarsch D, Derewenda U, Otlewski J, Derewenda ZS, Acta Crystallogr D Biol Crystallogr. 2004 Feb;60(Pt 2):275-80. Epub 2004, Jan 23. PMID:[http:// | + | The impact of Lys-->Arg surface mutations on the crystallization of the globular domain of RhoGDI., Czepas J, Devedjiev Y, Krowarsch D, Derewenda U, Otlewski J, Derewenda ZS, Acta Crystallogr D Biol Crystallogr. 2004 Feb;60(Pt 2):275-80. Epub 2004, Jan 23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14747703 14747703] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: protein crystallization; rational surface mutagenesis; rhogdi; high resolution; x-ray diffraction]] | [[Category: protein crystallization; rational surface mutagenesis; rhogdi; high resolution; x-ray diffraction]] | ||
| - | ''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 13:43:26 2008'' |
Revision as of 11:43, 20 March 2008
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| , resolution 1.60Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of RhoGDI K(199,200)R double mutant
Overview
The potential of rational surface mutagenesis for enhanced protein crystallization is being probed in an ongoing effort. In previous work, it was hypothesized that residues with high conformational entropy such as Glu and Lys are suitable targets for surface mutagenesis, as they are rarely incorporated in crystal contacts or protein-protein interfaces. Previous experiments using Lys-->Ala, Glu-->Ala and Glu-->Asp mutants confirmed that mutated proteins were more likely to crystallize. In the present paper, the usefulness of Lys-->Arg mutations is studied. Several mutations of the globular domain of human RhoGDI were generated, including the single mutants K105R, K113R, K127R, K138R and K141R, the double mutants K(98,99)R and K(199,200)R and the triple mutants K(98,99,105)R and K(135,138,141)R. It is shown that Lys-->Arg mutants are more likely to crystallize than the wild-type protein, although not as likely as Lys-->Ala mutants. Out of the nine mutants tested, five produced diffracting crystals, including the K(199,200)R double mutant, which crystallized in a new space group and exceeded by approximately 1.0 A the resolution of the diffraction of the wild-type crystal. Major crystal contacts in the new lattice were created by the mutated epitope.
About this Structure
1QVY is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The impact of Lys-->Arg surface mutations on the crystallization of the globular domain of RhoGDI., Czepas J, Devedjiev Y, Krowarsch D, Derewenda U, Otlewski J, Derewenda ZS, Acta Crystallogr D Biol Crystallogr. 2004 Feb;60(Pt 2):275-80. Epub 2004, Jan 23. PMID:14747703
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