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.


1uuy

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1uuy.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1uuy.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1uuy| PDB=1uuy | SCENE= }}
{{STRUCTURE_1uuy| PDB=1uuy | SCENE= }}
-
'''STRUCTURE OF A MOLYBDOPTERIN-BOUND CNX1G DOMAIN LINKS MOLYBDENUM AND COPPER METABOLISM'''
+
===STRUCTURE OF A MOLYBDOPTERIN-BOUND CNX1G DOMAIN LINKS MOLYBDENUM AND COPPER METABOLISM===
-
==Overview==
+
<!--
-
The molybdenum cofactor is part of the active site of all molybdenum-dependent enzymes, except nitrogenase. The molybdenum cofactor consists of molybdopterin, a phosphorylated pyranopterin, with an ene-dithiolate coordinating molybdenum. The same pyranopterin-based cofactor is involved in metal coordination of the homologous tungsten-containing enzymes found in archea. The molybdenum cofactor is synthesized by a highly conserved biosynthetic pathway. In plants, the multidomain protein Cnx1 catalyses the insertion of molybdenum into molybdopterin. The Cnx1 G domain (Cnx1G), whose crystal structure has been determined in its apo form, binds molybdopterin with high affinity and participates in the catalysis of molybdenum insertion. Here we present two high-resolution crystal structures of Cnx1G in complex with molybdopterin and with adenylated molybdopterin (molybdopterin-AMP), a mechanistically important intermediate. Molybdopterin-AMP is the reaction product of Cnx1G and is subsequently processed in a magnesium-dependent reaction by the amino-terminal E domain of Cnx1 to yield active molybdenum cofactor. The unexpected identification of copper bound to the molybdopterin dithiolate sulphurs in both structures, coupled with the observed copper inhibition of Cnx1G activity, provides a molecular link between molybdenum and copper metabolism.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15306815}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15306815 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15306815}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Chelatase]]
[[Category: Chelatase]]
[[Category: Molybdenum cofactor biosynthesis]]
[[Category: Molybdenum cofactor biosynthesis]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:43:44 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 12:22:21 2008''

Revision as of 09:22, 28 July 2008

Image:1uuy.png

Template:STRUCTURE 1uuy

STRUCTURE OF A MOLYBDOPTERIN-BOUND CNX1G DOMAIN LINKS MOLYBDENUM AND COPPER METABOLISM

Template:ABSTRACT PUBMED 15306815

About this Structure

1UUY is a Single protein structure of sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA.

Reference

Structure of the molybdopterin-bound Cnx1G domain links molybdenum and copper metabolism., Kuper J, Llamas A, Hecht HJ, Mendel RR, Schwarz G, Nature. 2004 Aug 12;430(7001):803-6. PMID:15306815

Page seeded by OCA on Mon Jul 28 12:22:21 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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