1GSW

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

1GSW の概要

• エントリーDOI: 10.2210/pdb1gsw/pdb
• 関連するPDBエントリー: 1D7E 1F98 1F9I 1GSV 1GSX 2PHY 2PYP 2PYR 3PHY 3PYP
• 分子名称: PHOTOACTIVE YELLOW PROTEIN, 4'-HYDROXYCINNAMIC ACID (3 entities in total)
• 機能のキーワード: photosynthesis, photoreceptor
• 由来する生物種: ECTOTHIORHODOSPIRA HALOPHILA
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14082.76

構造登録者

Van Aalten, D.M.F.,Crielaard, W.,Hellingwerf, K.J.,Joshua-Tor, L. (登録日: 2002-01-09, 公開日: 2002-02-14, 最終更新日: 2023-12-13)

主引用文献

Van Aalten, D.M.F.,Haker, A.,Hendriks, J.,Hellingwerf, K.J.,Joshua-Tor, L.,Crielaard, W.
Engineering Photocycle Dynamics: Crystal Structures and Kinetics of Three Photoactive Yellow Protein Hinge-Bending Mutants
J.Biol.Chem., 227:6438-, 2002

PubMed Abstract: 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.

PubMed: 11714713
DOI: 10.1074/JBC.M109313200

実験手法

X-RAY DIFFRACTION (1.85 Å)