1jro
From Proteopedia
(New page: 200px<br /><applet load="1jro" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jro, resolution 2.70Å" /> '''Crystal Structure of...) |
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| - | [[Image:1jro.gif|left|200px]]<br /><applet load="1jro" size=" | + | [[Image:1jro.gif|left|200px]]<br /><applet load="1jro" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1jro, resolution 2.70Å" /> | caption="1jro, resolution 2.70Å" /> | ||
'''Crystal Structure of Xanthine Dehydrogenase from Rhodobacter capsulatus'''<br /> | '''Crystal Structure of Xanthine Dehydrogenase from Rhodobacter capsulatus'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Xanthine dehydrogenase (XDH), a complex molybdo/iron-sulfur/flavoprotein, catalyzes the oxidation of hypoxanthine to xanthine followed by oxidation | + | Xanthine dehydrogenase (XDH), a complex molybdo/iron-sulfur/flavoprotein, catalyzes the oxidation of hypoxanthine to xanthine followed by oxidation of xanthine to uric acid with concomitant reduction of NAD+. The 2.7 A resolution structure of Rhodobacter capsulatus XDH reveals that the bacterial and bovine XDH have highly similar folds despite differences in subunit composition. The NAD+ binding pocket of the bacterial XDH resembles that of the dehydrogenase form of the bovine enzyme rather than that of the oxidase form, which reduces O(2) instead of NAD+. The drug allopurinol is used to treat XDH-catalyzed uric acid build-up occurring in gout or during cancer chemotherapy. As a hypoxanthine analog, it is oxidized to alloxanthine, which cannot be further oxidized but acts as a tight binding inhibitor of XDH. The 3.0 A resolution structure of the XDH-alloxanthine complex shows direct coordination of alloxanthine to the molybdenum via a nitrogen atom. These results provide a starting point for the rational design of new XDH inhibitors. |
==About this Structure== | ==About this Structure== | ||
| - | 1JRO is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rhodobacter_capsulatus Rhodobacter capsulatus] with CA, FES, MPN, MOS and FAD as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Xanthine_dehydrogenase Xanthine dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.17.1.4 1.17.1.4] Full crystallographic information is available from [http:// | + | 1JRO is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rhodobacter_capsulatus Rhodobacter capsulatus] with <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=FES:'>FES</scene>, <scene name='pdbligand=MPN:'>MPN</scene>, <scene name='pdbligand=MOS:'>MOS</scene> and <scene name='pdbligand=FAD:'>FAD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Xanthine_dehydrogenase Xanthine dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.17.1.4 1.17.1.4] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JRO OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Kisker, C.]] | [[Category: Kisker, C.]] | ||
[[Category: Leimkuhler, S.]] | [[Category: Leimkuhler, S.]] | ||
| - | [[Category: Rajagopalan, K | + | [[Category: Rajagopalan, K V.]] |
[[Category: Rappa, R.]] | [[Category: Rappa, R.]] | ||
[[Category: Theis, K.]] | [[Category: Theis, K.]] | ||
| - | [[Category: Truglio, J | + | [[Category: Truglio, J J.]] |
[[Category: CA]] | [[Category: CA]] | ||
[[Category: FAD]] | [[Category: FAD]] | ||
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[[Category: partial beta-barrel; xdh; xo]] | [[Category: partial beta-barrel; xdh; xo]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:26:00 2008'' |
Revision as of 11:26, 21 February 2008
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Crystal Structure of Xanthine Dehydrogenase from Rhodobacter capsulatus
Overview
Xanthine dehydrogenase (XDH), a complex molybdo/iron-sulfur/flavoprotein, catalyzes the oxidation of hypoxanthine to xanthine followed by oxidation of xanthine to uric acid with concomitant reduction of NAD+. The 2.7 A resolution structure of Rhodobacter capsulatus XDH reveals that the bacterial and bovine XDH have highly similar folds despite differences in subunit composition. The NAD+ binding pocket of the bacterial XDH resembles that of the dehydrogenase form of the bovine enzyme rather than that of the oxidase form, which reduces O(2) instead of NAD+. The drug allopurinol is used to treat XDH-catalyzed uric acid build-up occurring in gout or during cancer chemotherapy. As a hypoxanthine analog, it is oxidized to alloxanthine, which cannot be further oxidized but acts as a tight binding inhibitor of XDH. The 3.0 A resolution structure of the XDH-alloxanthine complex shows direct coordination of alloxanthine to the molybdenum via a nitrogen atom. These results provide a starting point for the rational design of new XDH inhibitors.
About this Structure
1JRO is a Protein complex structure of sequences from Rhodobacter capsulatus with , , , and as ligands. Active as Xanthine dehydrogenase, with EC number 1.17.1.4 Full crystallographic information is available from OCA.
Reference
Crystal structures of the active and alloxanthine-inhibited forms of xanthine dehydrogenase from Rhodobacter capsulatus., Truglio JJ, Theis K, Leimkuhler S, Rappa R, Rajagopalan KV, Kisker C, Structure. 2002 Jan;10(1):115-25. PMID:11796116
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