Tags

Type your tag names separated by a space and hit enter

Short hydrogen bonds in photoactive yellow protein.
Acta Crystallogr D Biol Crystallogr. 2004 Jun; 60(Pt 6):1008-16.AC

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.

Authors+Show Affiliations

Consortium for Advanced Radiation Sources, University of Chicago, USA. smander@midway.uchicago.eduNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, U.S. Gov't, P.H.S.

Language

eng

PubMed ID

15159559

Citation

Anderson, Spencer, et al. "Short Hydrogen Bonds in Photoactive Yellow Protein." Acta Crystallographica. Section D, Biological Crystallography, vol. 60, no. Pt 6, 2004, pp. 1008-16.
Anderson S, Crosson S, Moffat K. Short hydrogen bonds in photoactive yellow protein. Acta Crystallogr D Biol Crystallogr. 2004;60(Pt 6):1008-16.
Anderson, S., Crosson, S., & Moffat, K. (2004). Short hydrogen bonds in photoactive yellow protein. Acta Crystallographica. Section D, Biological Crystallography, 60(Pt 6), 1008-16.
Anderson S, Crosson S, Moffat K. Short Hydrogen Bonds in Photoactive Yellow Protein. Acta Crystallogr D Biol Crystallogr. 2004;60(Pt 6):1008-16. PubMed PMID: 15159559.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Short hydrogen bonds in photoactive yellow protein. AU - Anderson,Spencer, AU - Crosson,Sean, AU - Moffat,Keith, Y1 - 2004/05/21/ PY - 2004/01/09/received PY - 2004/03/15/accepted PY - 2004/5/26/pubmed PY - 2005/2/3/medline PY - 2004/5/26/entrez SP - 1008 EP - 16 JF - Acta crystallographica. Section D, Biological crystallography JO - Acta Crystallogr D Biol Crystallogr VL - 60 IS - Pt 6 N2 - 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. SN - 0907-4449 UR - https://www.unboundmedicine.com/medline/citation/15159559/Short_hydrogen_bonds_in_photoactive_yellow_protein_ L2 - http://scripts.iucr.org/cgi-bin/paper?S090744490400616X DB - PRIME DP - Unbound Medicine ER -