1qvy
From Proteopedia
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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 with as ligand. 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 Fri Feb 15 16:46:07 2008
