1qvy
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1qvy.jpg|left|200px]] | [[Image:1qvy.jpg|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1qvy", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | + | --> | |
| - | + | {{STRUCTURE_1qvy| PDB=1qvy | SCENE= }} | |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''Crystal structure of RhoGDI K(199,200)R double mutant''' | '''Crystal structure of RhoGDI K(199,200)R double mutant''' | ||
| Line 30: | Line 27: | ||
[[Category: Devedjiev, Y.]] | [[Category: Devedjiev, Y.]] | ||
[[Category: Krowarsh, D.]] | [[Category: Krowarsh, D.]] | ||
| - | [[Category: | + | [[Category: High resolution]] |
| - | [[Category: | + | [[Category: Protein crystallization]] |
| - | [[Category: | + | [[Category: Rational surface mutagenesis]] |
| - | [[Category: | + | [[Category: Rhogdi]] |
| - | [[Category: | + | [[Category: X-ray diffraction]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:45:40 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 03:45, 3 May 2008
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 Page seeded by OCA on Sat May 3 06:45:40 2008
