2nox: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:2nox.gif|left|200px]] | [[Image:2nox.gif|left|200px]] | ||
'''Crystal structure of tryptophan 2,3-dioxygenase from Ralstonia metallidurans''' | {{Structure | ||
|PDB= 2nox |SIZE=350|CAPTION= <scene name='initialview01'>2nox</scene>, resolution 2.400Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN IX CONTAINING FE'>HEM</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Tryptophan_2,3-dioxygenase Tryptophan 2,3-dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.11 1.13.11.11] | |||
|GENE= | |||
}} | |||
'''Crystal structure of tryptophan 2,3-dioxygenase from Ralstonia metallidurans''' | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
2NOX is a [ | 2NOX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Cupriavidus_metallidurans Cupriavidus metallidurans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NOX OCA]. | ||
==Reference== | ==Reference== | ||
Crystal structure and mechanism of tryptophan 2,3-dioxygenase, a heme enzyme involved in tryptophan catabolism and in quinolinate biosynthesis., Zhang Y, Kang SA, Mukherjee T, Bale S, Crane BR, Begley TP, Ealick SE, Biochemistry. 2007 Jan 9;46(1):145-55. PMID:[http:// | Crystal structure and mechanism of tryptophan 2,3-dioxygenase, a heme enzyme involved in tryptophan catabolism and in quinolinate biosynthesis., Zhang Y, Kang SA, Mukherjee T, Bale S, Crane BR, Begley TP, Ealick SE, Biochemistry. 2007 Jan 9;46(1):145-55. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17198384 17198384] | ||
[[Category: Cupriavidus metallidurans]] | [[Category: Cupriavidus metallidurans]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 25: | Line 34: | ||
[[Category: heme protein]] | [[Category: heme protein]] | ||
''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 17:49:09 2008'' | ||
Revision as of 18:49, 20 March 2008
| |||||||
| , resolution 2.400Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Tryptophan 2,3-dioxygenase, with EC number 1.13.11.11 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of tryptophan 2,3-dioxygenase from Ralstonia metallidurans
OverviewOverview
The structure of tryptophan 2,3-dioxygenase (TDO) from Ralstonia metallidurans was determined at 2.4 A. TDO catalyzes the irreversible oxidation of l-tryptophan to N-formyl kynurenine, which is the initial step in tryptophan catabolism. TDO is a heme-containing enzyme and is highly specific for its substrate l-tryptophan. The structure is a tetramer with a heme cofactor bound at each active site. The monomeric fold, as well as the heme binding site, is similar to that of the large domain of indoleamine 2,3-dioxygenase, an enzyme that catalyzes the same reaction except with a broader substrate tolerance. Modeling of the putative (S)-tryptophan hydroperoxide intermediate into the active site, as well as substrate analogue and mutagenesis studies, are consistent with a Criegee mechanism for the reaction.
About this StructureAbout this Structure
2NOX is a Single protein structure of sequence from Cupriavidus metallidurans. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure and mechanism of tryptophan 2,3-dioxygenase, a heme enzyme involved in tryptophan catabolism and in quinolinate biosynthesis., Zhang Y, Kang SA, Mukherjee T, Bale S, Crane BR, Begley TP, Ealick SE, Biochemistry. 2007 Jan 9;46(1):145-55. PMID:17198384
Page seeded by OCA on Thu Mar 20 17:49:09 2008