1otd

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{{STRUCTURE_1otd| PDB=1otd | SCENE= }}
{{STRUCTURE_1otd| PDB=1otd | SCENE= }}
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'''STRONG HYDROGEN BONDS IN PHOTOACTIVE YELLOW PROTEIN AND THEIR ROLE IN ITS PHOTOCYCLE'''
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===STRONG HYDROGEN BONDS IN PHOTOACTIVE YELLOW PROTEIN AND THEIR ROLE IN ITS PHOTOCYCLE===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 15159559 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15159559}}
==About this Structure==
==About this Structure==
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[[Category: Moffat, K.]]
[[Category: Moffat, K.]]
[[Category: Pyp]]
[[Category: Pyp]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:15:38 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 21:20:43 2008''

Revision as of 18:20, 28 July 2008

Image:1otd.png

Template:STRUCTURE 1otd

STRONG HYDROGEN BONDS IN PHOTOACTIVE YELLOW PROTEIN AND THEIR ROLE IN ITS PHOTOCYCLE

Template:ABSTRACT PUBMED 15159559

About this Structure

1OTD is a Single protein structure of sequence from Halorhodospira halophila. Full crystallographic information is available from OCA.

Reference

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

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