1otb: Difference between revisions

Revision as of 15:21, 21 February 2008

WILD TYPE PHOTOACTIVE YELLOW PROTEIN, P63 AT 295K

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

1OTB is a Single protein structure of sequence from Halorhodospira halophila with as ligand. 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 Feb 21 14:21:22 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1otb.jpg|left|200px]]<br /><applet load="1otb" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1otb.jpg|left|200px]]<br /><applet load="1otb" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1otb, resolution 1.10&Aring;" />
 '''WILD TYPE PHOTOACTIVE YELLOW PROTEIN, P63 AT 295K'''<br />
 ==Overview==
-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.
+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 Structure==
-OTB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Halorhodospira_halophila Halorhodospira halophila] with HC4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OTB OCA].
+OTB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Halorhodospira_halophila Halorhodospira halophila] with <scene name='pdbligand=HC4:'>HC4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OTB OCA].
 ==Reference==
@@ Line 19: / Line 19: @@
 [[Category: pyp]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:10:49 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:21:22 2008''