1gsw

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1gsw, resolution 1.85Å

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CRYSTAL STRUCTURE OF THE P65 CRYSTAL FORM OF PHOTOACTIVE YELLOW PROTEIN G51S MUTANT

Overview

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

1GSW is a Single protein structure of sequence from Halorhodospira halophila with HC4 as ligand. Structure known Active Site: HC4. Full crystallographic information is available from OCA.

Reference

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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