1jro
From Proteopedia
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|PDB= 1jro |SIZE=350|CAPTION= <scene name='initialview01'>1jro</scene>, resolution 2.70Å | |PDB= 1jro |SIZE=350|CAPTION= <scene name='initialview01'>1jro</scene>, resolution 2.70Å | ||
|SITE= | |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> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=MOS:DIOXOTHIOMOLYBDENUM(VI)+ION'>MOS</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> |
| - | + | |ACTIVITY= <span class='plainlinks'>[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] </span> | |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1jrp|1JRP]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jro FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jro OCA], [http://www.ebi.ac.uk/pdbsum/1jro PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1jro RCSB]</span> | ||
}} | }} | ||
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[[Category: Theis, K.]] | [[Category: Theis, K.]] | ||
[[Category: Truglio, J J.]] | [[Category: Truglio, J J.]] | ||
| - | [[Category: | + | [[Category: partial beta-barrel]] |
| - | [[Category: | + | [[Category: xdh]] |
| - | [[Category: | + | [[Category: xo]] |
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:38:01 2008'' |
Revision as of 18:38, 30 March 2008
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| , resolution 2.70Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , , | ||||||
| Activity: | Xanthine dehydrogenase, with EC number 1.17.1.4 | ||||||
| Related: | 1JRP
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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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