1gsv: Difference between revisions
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==Overview== | ==Overview== | ||
Crystallographic and spectroscopic analyses of three hinge-bending mutants | 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. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Halorhodospira halophila]] | [[Category: Halorhodospira halophila]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Aalten, D | [[Category: Aalten, D M.F Van.]] | ||
[[Category: Crielaard, W.]] | [[Category: Crielaard, W.]] | ||
[[Category: Hellingwerf, K | [[Category: Hellingwerf, K J.]] | ||
[[Category: Joshua-Tor, L.]] | [[Category: Joshua-Tor, L.]] | ||
[[Category: HC4]] | [[Category: HC4]] | ||
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[[Category: photosynthesis]] | [[Category: photosynthesis]] | ||
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Revision as of 13:53, 21 February 2008
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CRYSTAL STRUCTURE OF THE P65 CRYSTAL FORM OF PHOTOACTIVE YELLOW PROTEIN G47S MUTANT
OverviewOverview
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.
About this StructureAbout this Structure
1GSV is a Single protein structure of sequence from Halorhodospira halophila with as ligand. Known structural/functional Site: . Full crystallographic information is available from OCA.
ReferenceReference
Engineering photocycle dynamics. Crystal structures and kinetics of three photoactive yellow protein hinge-bending mutants., van Aalten DM, Haker A, Hendriks J, Hellingwerf KJ, Joshua-Tor L, Crielaard W, J Biol Chem. 2002 Feb 22;277(8):6463-8. Epub 2001 Nov 19. PMID:11714713
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