2agl
From Proteopedia
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| - | [[Image:2agl.gif|left|200px]] | + | [[Image:2agl.gif|left|200px]] |
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| - | '''Crystal structure of the phenylhydrazine adduct of aromatic amine dehydrogenase from Alcaligenes faecalis''' | + | {{Structure |
| + | |PDB= 2agl |SIZE=350|CAPTION= <scene name='initialview01'>2agl</scene>, resolution 1.400Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=PHZ:1-PHENYLHYDRAZINE'>PHZ</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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of the phenylhydrazine adduct of aromatic amine dehydrogenase from Alcaligenes faecalis''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2AGL is a [ | + | 2AGL is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Alcaligenes_faecalis Alcaligenes faecalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AGL OCA]. |
==Reference== | ==Reference== | ||
| - | Atomic description of an enzyme reaction dominated by proton tunneling., Masgrau L, Roujeinikova A, Johannissen LO, Hothi P, Basran J, Ranaghan KE, Mulholland AJ, Sutcliffe MJ, Scrutton NS, Leys D, Science. 2006 Apr 14;312(5771):237-41. PMID:[http:// | + | Atomic description of an enzyme reaction dominated by proton tunneling., Masgrau L, Roujeinikova A, Johannissen LO, Hothi P, Basran J, Ranaghan KE, Mulholland AJ, Sutcliffe MJ, Scrutton NS, Leys D, Science. 2006 Apr 14;312(5771):237-41. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16614214 16614214] |
[[Category: Alcaligenes faecalis]] | [[Category: Alcaligenes faecalis]] | ||
[[Category: Aralkylamine dehydrogenase]] | [[Category: Aralkylamine dehydrogenase]] | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''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 15:49:29 2008'' |
Revision as of 13:49, 20 March 2008
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| , resolution 1.400Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Aralkylamine dehydrogenase, with EC number 1.4.99.4 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the phenylhydrazine adduct of aromatic amine dehydrogenase from Alcaligenes faecalis
Overview
We present an atomic-level description of the reaction chemistry of an enzyme-catalyzed reaction dominated by proton tunneling. By solving structures of reaction intermediates at near-atomic resolution, we have identified the reaction pathway for tryptamine oxidation by aromatic amine dehydrogenase. Combining experiment and computer simulation, we show proton transfer occurs predominantly to oxygen O2 of Asp(128)beta in a reaction dominated by tunneling over approximately 0.6 angstroms. The role of long-range coupled motions in promoting tunneling is controversial. We show that, in this enzyme system, tunneling is promoted by a short-range motion modulating proton-acceptor distance and no long-range coupled motion is required.
About this Structure
2AGL is a Protein complex structure of sequences from Alcaligenes faecalis. Full crystallographic information is available from OCA.
Reference
Atomic description of an enzyme reaction dominated by proton tunneling., Masgrau L, Roujeinikova A, Johannissen LO, Hothi P, Basran J, Ranaghan KE, Mulholland AJ, Sutcliffe MJ, Scrutton NS, Leys D, Science. 2006 Apr 14;312(5771):237-41. PMID:16614214
Page seeded by OCA on Thu Mar 20 15:49:29 2008
