This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1ot6

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1ot6.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1ot6.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1ot6| PDB=1ot6 | SCENE= }}
{{STRUCTURE_1ot6| PDB=1ot6 | SCENE= }}
-
'''CRYOTRAPPED CRYSTAL STRUCTURE OF THE E46Q MUTANT OF PHOTOACTIVE YELLOW PROTEIN UNDER CONTINUOUS ILLUMINATION AT 110K'''
+
===CRYOTRAPPED CRYSTAL STRUCTURE OF THE E46Q MUTANT OF PHOTOACTIVE YELLOW PROTEIN UNDER CONTINUOUS ILLUMINATION AT 110K===
-
==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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15159559}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15159559 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15159559}}
==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Cryotrapping]]
[[Category: Cryotrapping]]
[[Category: Pyp]]
[[Category: Pyp]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:15:16 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 10 12:40:15 2008''

Revision as of 09:40, 10 July 2008

Image:1ot6.png

Template:STRUCTURE 1ot6

CRYOTRAPPED CRYSTAL STRUCTURE OF THE E46Q MUTANT OF PHOTOACTIVE YELLOW PROTEIN UNDER CONTINUOUS ILLUMINATION AT 110K

Template:ABSTRACT PUBMED 15159559

About this Structure

1OT6 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

Page seeded by OCA on Thu Jul 10 12:40:15 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ot6"
Personal tools