1jro
From Proteopedia
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| - | [[Image:1jro.gif|left|200px]] | + | [[Image:1jro.gif|left|200px]] |
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| - | '''Crystal Structure of Xanthine Dehydrogenase from Rhodobacter capsulatus''' | + | {{Structure |
| + | |PDB= 1jro |SIZE=350|CAPTION= <scene name='initialview01'>1jro</scene>, resolution 2.70Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=MPN:PHOSPHORIC+ACID+MONO-(2-AMINO-4-OXO-5,6-DITHIOXO-1,5,6,7,8A,9,10,10A-OCTAHYDRO-4H-8-OXA-1,3,9,10-TETRAAZA-ANTHRACEN-7-YLMETHYL)+ESTER'>MPN</scene>, <scene name='pdbligand=MOS:DIOXOTHIOMOLYBDENUM(VI)+ION'>MOS</scene> and <scene name='pdbligand=FAD:FLAVIN-ADENINE DINUCLEOTIDE'>FAD</scene> | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Crystal Structure of Xanthine Dehydrogenase from Rhodobacter capsulatus''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1JRO is a [ | + | 1JRO is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Rhodobacter_capsulatus Rhodobacter capsulatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JRO OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11796116 11796116] |
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Rhodobacter capsulatus]] | [[Category: Rhodobacter capsulatus]] | ||
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[[Category: partial beta-barrel; xdh; xo]] | [[Category: partial beta-barrel; xdh; xo]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:07:29 2008'' |
Revision as of 10:07, 20 March 2008
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| , resolution 2.70Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , and | ||||||
| Activity: | Xanthine dehydrogenase, with EC number 1.17.1.4 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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