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.


2d1e

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2d1e.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2d1e.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2d1e| PDB=2d1e | SCENE= }}
{{STRUCTURE_2d1e| PDB=2d1e | SCENE= }}
-
'''Crystal structure of PcyA-biliverdin complex'''
+
===Crystal structure of PcyA-biliverdin complex===
-
==Overview==
+
<!--
-
Phytobilins (light harvesting and photoreceptor pigments in higher plants, algae, and cyanobacteria) are synthesized from biliverdin IXalpha (BV) by ferredoxin-dependent bilin reductases (FDBRs). Phycocyanobilin:ferredoxin oxidoreductase (PcyA), one such FDBR, is a new class of radical enzymes that require neither cofactors nor metals and serially reduces the vinyl group of the D-ring and A-ring of BV using four electrons from ferredoxin to produce phycocyanobilin, one of the phytobilins. We have determined the crystal structure of PcyA from Synechocystis sp. PCC 6803 in complex with BV, revealing the first tertiary structure of an FDBR family member. PcyA is folded in a three-layer alpha/beta/alpha sandwich structure, in which BV in a cyclic conformation is positioned between the beta-sheet and C-terminal alpha-helices. The basic patch on the PcyA surface near the BV molecule may provide a binding site for acidic ferredoxin, allowing direct transfer of electrons to BV. The orientation of BV is definitely fixed in PcyA by several hydrophilic interactions and the shape of the BV binding pocket of PcyA. We propose the mechanism by which the sequential reduction of the D- and A-rings is controlled, where Asp-105, located between the two reduction sites, would play the central role by changing its conformation during the reaction. Homology modeling of other FDBRs based on the PcyA structure fits well with previous genetic and biochemical data, thereby providing a structural basis for the reaction mechanism of FDBRs.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16380422}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16380422 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16380422}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Alpha-beta-alpha sandwich]]
[[Category: Alpha-beta-alpha sandwich]]
[[Category: Enzyme-substrate complex]]
[[Category: Enzyme-substrate complex]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 23:30:35 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 19:00:27 2008''

Revision as of 16:00, 27 July 2008

Image:2d1e.png

Template:STRUCTURE 2d1e

Crystal structure of PcyA-biliverdin complex

Template:ABSTRACT PUBMED 16380422

About this Structure

2D1E is a Single protein structure of sequence from Synechocystis sp.. Full crystallographic information is available from OCA.

Reference

Crystal structure of phycocyanobilin:ferredoxin oxidoreductase in complex with biliverdin IXalpha, a key enzyme in the biosynthesis of phycocyanobilin., Hagiwara Y, Sugishima M, Takahashi Y, Fukuyama K, Proc Natl Acad Sci U S A. 2006 Jan 3;103(1):27-32. Epub 2005 Dec 27. PMID:16380422

Page seeded by OCA on Sun Jul 27 19:00:27 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2d1e"
Personal tools