1gsv: Difference between revisions

Crystallographic and spectroscopic analyses of three hinge-bending mutants, of the photoactive yellow protein are described. Previous studies have, identified Gly(47) and Gly(51) as possible hinge points in the structure, of the protein, allowing backbone segments around the chromophore to, undergo large concerted motions. We have designed, crystallized, and, solved the structures of three mutants: G47S, G51S, and G47S/G51S. The, protein dynamics of these mutants are significantly affected. Transitions, in the photocycle, measured with laser induced transient absorption, spectroscopy, show rates up to 6-fold different from the wild type protein, and show an additive effect in the double mutant. Compared with the native, structure, no significant conformational differences were observed in the, structures of the mutant proteins. We conclude that the structural and, dynamic integrity of the region around these mutations is of crucial, importance to the photocycle and suggest that the hinge-bending properties, of Gly(51) may also play a role in PAS domain proteins where it is one of, the few conserved residues.

1GSV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Halorhodospira_halophila Halorhodospira halophila] with HC4 as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Site: HC4. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GSV OCA].  

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