1uux
From Proteopedia
(New page: 200px<br /><applet load="1uux" size="450" color="white" frame="true" align="right" spinBox="true" caption="1uux, resolution 1.60Å" /> '''STRUCTURE OF A MOLYB...) |
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| - | [[Image:1uux.jpg|left|200px]]<br /><applet load="1uux" size=" | + | [[Image:1uux.jpg|left|200px]]<br /><applet load="1uux" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1uux, resolution 1.60Å" /> | caption="1uux, resolution 1.60Å" /> | ||
'''STRUCTURE OF A MOLYBDOPTERIN-BOUND CNX1G DOMAIN LINKS MOLYBDENUM AND COPPER METABOLISM'''<br /> | '''STRUCTURE OF A MOLYBDOPTERIN-BOUND CNX1G DOMAIN LINKS MOLYBDENUM AND COPPER METABOLISM'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The molybdenum cofactor is part of the active site of all | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1UUX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana] with CU1, MTE, PPI, IMD and FMT as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1UUX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana] with <scene name='pdbligand=CU1:'>CU1</scene>, <scene name='pdbligand=MTE:'>MTE</scene>, <scene name='pdbligand=PPI:'>PPI</scene>, <scene name='pdbligand=IMD:'>IMD</scene> and <scene name='pdbligand=FMT:'>FMT</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UUX OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Arabidopsis thaliana]] | [[Category: Arabidopsis thaliana]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Hecht, H | + | [[Category: Hecht, H J.]] |
[[Category: Kuper, J.]] | [[Category: Kuper, J.]] | ||
[[Category: Llamas, A.]] | [[Category: Llamas, A.]] | ||
| - | [[Category: Mendel, R | + | [[Category: Mendel, R R.]] |
[[Category: Schwarz, G.]] | [[Category: Schwarz, G.]] | ||
[[Category: CU1]] | [[Category: CU1]] | ||
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[[Category: molybdenum cofactor biosynthesis]] | [[Category: molybdenum cofactor biosynthesis]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:28:37 2008'' |
Revision as of 13:28, 21 February 2008
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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.
About this Structure
1UUX is a Single protein structure of sequence from Arabidopsis thaliana with , , , and as ligands. 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 Thu Feb 21 15:28:37 2008
Categories: Arabidopsis thaliana | Single protein | Hecht, H J. | Kuper, J. | Llamas, A. | Mendel, R R. | Schwarz, G. | CU1 | FMT | IMD | MTE | PPI | Chelatase | Molybdenum cofactor biosynthesis
