2oiz: Difference between revisions
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|PDB= 2oiz |SIZE=350|CAPTION= <scene name='initialview01'>2oiz</scene>, resolution 1.050Å | |PDB= 2oiz |SIZE=350|CAPTION= <scene name='initialview01'>2oiz</scene>, resolution 1.050Å | ||
|SITE= <scene name='pdbsite=AC1:Tsr+Binding+Site+For+Residue+H+1701'>AC1</scene>, <scene name='pdbsite=AC2:Tsr+Binding+Site+For+Residue+D+1702'>AC2</scene> and <scene name='pdbsite=AC3:Pg4+Binding+Site+For+Residue+A+1700'>AC3</scene> | |SITE= <scene name='pdbsite=AC1:Tsr+Binding+Site+For+Residue+H+1701'>AC1</scene>, <scene name='pdbsite=AC2:Tsr+Binding+Site+For+Residue+D+1702'>AC2</scene> and <scene name='pdbsite=AC3:Pg4+Binding+Site+For+Residue+A+1700'>AC3</scene> | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=TRQ:2-AMINO-3-(6,7-DIOXO-6,7-DIHYDRO-1H-INDOL-3-YL)-PROPIONIC+ACID'>TRQ</scene>, <scene name='pdbligand=TSR:2-(1H-INDOL-3-YL)ACETAMIDE'>TSR</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Aralkylamine_dehydrogenase Aralkylamine dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.99.4 1.4.99.4] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Aralkylamine_dehydrogenase Aralkylamine dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.99.4 1.4.99.4] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2oiz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oiz OCA], [http://www.ebi.ac.uk/pdbsum/2oiz PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2oiz RCSB]</span> | |||
}} | }} | ||
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[[Category: Leys, D.]] | [[Category: Leys, D.]] | ||
[[Category: Roujeinikova, A.]] | [[Category: Roujeinikova, A.]] | ||
[[Category: h-tunneling]] | [[Category: h-tunneling]] | ||
[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
[[Category: tryptophan tryptophyl quinone]] | [[Category: tryptophan tryptophyl quinone]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:18:34 2008'' | ||
Revision as of 04:18, 31 March 2008
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| , resolution 1.050Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , and | ||||||
| Ligands: | , , | ||||||
| Activity: | Aralkylamine dehydrogenase, with EC number 1.4.99.4 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of the Tryptamine-Derived (Indol-3-Acetamide)-TTQ Adduct of Aromatic Amine Dehydrogenase
OverviewOverview
Aromatic amine dehydrogenase uses a tryptophan tryptophylquinone (TTQ) cofactor to oxidatively deaminate primary aromatic amines. In the reductive half-reaction, a proton is transferred from the substrate C1 to betaAsp-128 O-2, in a reaction that proceeds by H-tunneling. Using solution studies, kinetic crystallography, and computational simulation we show that the mechanism of oxidation of aromatic carbinolamines is similar to amine oxidation, but that carbinolamine oxidation occurs at a substantially reduced rate. This has enabled us to determine for the first time the structure of the intermediate prior to the H-transfer/reduction step. The proton-betaAsp-128 O-2 distance is approximately 3.7A, in contrast to the distance of approximately 2.7A predicted for the intermediate formed with the corresponding primary amine substrate. This difference of approximately 1.0 A is due to an unexpected conformation of the substrate moiety, which is supported by molecular dynamic simulations and reflected in the approximately 10(7)-fold slower TTQ reduction rate with phenylaminoethanol compared with that with primary amines. A water molecule is observed near TTQ C-6 and is likely derived from the collapse of the preceding carbinolamine TTQ-adduct. We suggest this water molecule is involved in consecutive proton transfers following TTQ reduction, and is ultimately repositioned near the TTQ O-7 concomitant with protein rearrangement. For all carbinolamines tested, highly stable amide-TTQ adducts are formed following proton abstraction and TTQ reduction. Slow hydrolysis of the amide occurs after, rather than prior to, TTQ oxidation and leads ultimately to a carboxylic acid product.
About this StructureAbout this Structure
2OIZ is a Protein complex structure of sequences from Alcaligenes faecalis. Full crystallographic information is available from OCA.
ReferenceReference
New insights into the reductive half-reaction mechanism of aromatic amine dehydrogenase revealed by reaction with carbinolamine substrates., Roujeinikova A, Hothi P, Masgrau L, Sutcliffe MJ, Scrutton NS, Leys D, J Biol Chem. 2007 Aug 17;282(33):23766-77. Epub 2007 May 1. PMID:17475620
Page seeded by OCA on Mon Mar 31 04:18:34 2008