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1jro

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|PDB= 1jro |SIZE=350|CAPTION= <scene name='initialview01'>1jro</scene>, resolution 2.70&Aring;
|PDB= 1jro |SIZE=350|CAPTION= <scene name='initialview01'>1jro</scene>, resolution 2.70&Aring;
|SITE=
|SITE=
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|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>
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|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>
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|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]
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|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=
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|DOMAIN=
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|RELATEDENTRY=[[1jrp|1JRP]]
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|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.]]
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[[Category: CA]]
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[[Category: partial beta-barrel]]
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[[Category: FAD]]
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[[Category: xdh]]
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[[Category: FES]]
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[[Category: xo]]
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[[Category: MOS]]
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[[Category: MPN]]
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[[Category: partial beta-barrel; xdh; xo]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:07:29 2008''
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''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


PDB ID 1jro

Drag the structure with the mouse to rotate
, 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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