1OTB

WILD TYPE PHOTOACTIVE YELLOW PROTEIN, P63 AT 295K

1OTB の概要

• エントリーDOI: 10.2210/pdb1otb/pdb
• 関連するPDBエントリー: 1OTA 2PHY
• 分子名称: Photoactive yellow protein, 4'-HYDROXYCINNAMIC ACID (3 entities in total)
• 機能のキーワード: pyp, signaling protein
• 由来する生物種: Halorhodospira halophila
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14052.73

構造登録者

Anderson, S.,Crosson, S.,Moffat, K. (登録日: 2003-03-21, 公開日: 2004-05-11, 最終更新日: 2023-08-16)

主引用文献

Anderson, S.,Crosson, S.,Moffat, K.
Short hydrogen bonds in photoactive yellow protein.
Acta Crystallogr.,Sect.D, 60:1008-1016, 2004

PubMed Abstract: Eight high-resolution crystal structures of the ground state of photoactive yellow protein (PYP) solved under a variety of conditions reveal that its chromophore is stabilized by two unusually short hydrogen bonds. Both Tyr42 Oeta and Glu46 Oepsilon are separated from the chromophore phenolate oxygen by less than the sum of their atomic van der Waals radii, 2.6 angstroms. This is characteristic of strong hydrogen bonding, in which hydrogen bonds acquire significant covalent character. The hydrogen bond from the protonated Glu46 to the negatively charged phenolate oxygen is 2.58 +/- 0.01 angstroms in length, while that from Tyr42 is considerably shorter, 2.49 +/- 0.01 angstroms. The E46Q mutant was solved to 0.95 angstroms resolution; the isosteric mutation increased the length of the hydrogen bond from Glx46 to the chromophore by 0.29 +/- 0.01 angstroms to that of an average hydrogen bond, 2.88 +/- 0.01 angstroms. The very short hydrogen bond from Tyr42 explains why mutating this residue has such a severe effect on the ground-state structure and PYP photocycle. The effect of isosteric mutations on the photocycle can be largely explained by the alterations to the length and strength of these hydrogen bonds.

PubMed: 15159559
DOI: 10.1107/S090744490400616X

実験手法

X-RAY DIFFRACTION (1.1 Å)