1uwp: Difference between revisions

Revision as of 16:38, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1uwp.png

Template:STRUCTURE 1uwp

INITIAL EVENTS IN THE PHOTOCYCLE OF PHOTOACTIVE YELLOW PROTEININITIAL EVENTS IN THE PHOTOCYCLE OF PHOTOACTIVE YELLOW PROTEIN

Template:ABSTRACT PUBMED 15026418

About this StructureAbout this Structure

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

ReferenceReference

Initial events in the photocycle of photoactive yellow protein., Kort R, Hellingwerf KJ, Ravelli RB, J Biol Chem. 2004 Jun 18;279(25):26417-24. Epub 2004 Mar 16. PMID:15026418

Page seeded by OCA on Sun Jul 27 16:37:57 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:1uwp.gif|left|200px]]
+{{Seed}}
+[[Image:1uwp.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1uwp|  PDB=1uwp  |  SCENE=  }}
-'''INITIAL EVENTS IN THE PHOTOCYCLE OF PHOTOACTIVE YELLOW PROTEIN'''
+===INITIAL EVENTS IN THE PHOTOCYCLE OF PHOTOACTIVE YELLOW PROTEIN===
-==Overview==
+<!--
-The light-induced isomerization of a double bond is the key event that allows the conversion of light energy into a structural change in photoactive proteins for many light-mediated biological processes, such as vision, photosynthesis, photomorphogenesis, and photo movement. Cofactors such as retinals, linear tetrapyrroles, and 4-hydroxy-cinnamic acid have been selected by nature that provide the essential double bond to transduce the light signal into a conformational change and eventually, a physiological response. Here we report the first events after light excitation of the latter chromophore, containing a single ethylene double bond, in a low temperature crystallographic study of the photoactive yellow protein. We measured experimental phases to overcome possible model bias, corrected for minimized radiation damage, and measured absorption spectra of crystals to analyze the photoproducts formed. The data show a mechanism for the light activation of photoactive yellow protein, where the energy to drive the remainder of the conformational changes is stored in a slightly strained but fully cis-chromophore configuration. In addition, our data indicate a role for backbone rearrangements during the very early structural events.
+The line below this paragraph, {{ABSTRACT_PUBMED_15026418}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15026418 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15026418}}
 ==About this Structure==
@@ Line 34: / Line 38: @@
 [[Category: Signaling protein]]
 [[Category: Yellow]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 11:47:12 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 16:37:57 2008''