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.


2dke

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2dke.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2dke.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2dke| PDB=2dke | SCENE= }}
{{STRUCTURE_2dke| PDB=2dke | SCENE= }}
-
'''Crystal structure of substrate-free form of PcyA'''
+
===Crystal structure of substrate-free form of PcyA===
-
==Overview==
+
<!--
-
Phycocyanobilin:ferredoxin oxidoreductase (PcyA) catalyzes the sequential reduction of the vinyl group of the D-ring and the A-ring of biliverdin IXalpha (BV) using ferredoxin to produce phycocyanobilin, a pigment used for light-harvesting and light-sensing in red algae and cyanobacteria. We have determined the crystal structure of the substrate-free form of PcyA from Synechocystis sp. PCC 6803 at 2.5 A resolution. Structural comparison of the substrate-free form and the PcyA-BV complex shows major changes around the entrance of the BV binding pocket; upon BV binding, two alpha-helices and nearby side-chains move to produce tight BV binding. Unexpectedly, these movements localize the positive charges around the BV binding site, which may contribute to the proper binding of ferredoxin to PcyA. In the substrate-free form, the side-chain of Asp105 was located at a site that would be underneath the BV A-ring in the PcyA-BV complex and hydrogen-bonded with His88. We propose that BV is protonated by a mechanism involving conformational changes of these two residues before reduction.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16782089}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16782089 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16782089}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Alpha-beta-alpha sandwich]]
[[Category: Alpha-beta-alpha sandwich]]
[[Category: Substrate free form]]
[[Category: Substrate free form]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 00:36:36 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 14:15:14 2008''

Revision as of 11:15, 29 July 2008

Image:2dke.png

Template:STRUCTURE 2dke

Crystal structure of substrate-free form of PcyA

Template:ABSTRACT PUBMED 16782089

About this Structure

2DKE is a Single protein structure of sequence from Synechocystis sp.. Full crystallographic information is available from OCA.

Reference

Induced-fitting and electrostatic potential change of PcyA upon substrate binding demonstrated by the crystal structure of the substrate-free form., Hagiwara Y, Sugishima M, Takahashi Y, Fukuyama K, FEBS Lett. 2006 Jul 10;580(16):3823-8. Epub 2006 Jun 12. PMID:16782089

Page seeded by OCA on Tue Jul 29 14:15:14 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2dke"
Personal tools