1ot6
CRYOTRAPPED CRYSTAL STRUCTURE OF THE E46Q MUTANT OF PHOTOACTIVE YELLOW PROTEIN UNDER CONTINUOUS ILLUMINATION AT 110K
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| , resolution 0.95Å | |||||||
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| Ligands: | |||||||
| Gene: | PYP (Halorhodospira halophila) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
OverviewOverview
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.
About this StructureAbout this Structure
1OT6 is a Single protein structure of sequence from Halorhodospira halophila. Full crystallographic information is available from OCA.
ReferenceReference
Short hydrogen bonds in photoactive yellow protein., Anderson S, Crosson S, Moffat K, Acta Crystallogr D Biol Crystallogr. 2004 Jun;60(Pt 6):1008-16. Epub 2004, May 21. PMID:15159559
Page seeded by OCA on Thu Mar 20 13:15:16 2008