2agy
From Proteopedia
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[[Image:2agy.gif|left|200px]] | [[Image:2agy.gif|left|200px]] | ||
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'''Crystal structure of the Schiff base intermediate in the reductive half-reaction of aromatic amine dehydrogenase (AADH) with tryptamine. Monoclinic form''' | '''Crystal structure of the Schiff base intermediate in the reductive half-reaction of aromatic amine dehydrogenase (AADH) with tryptamine. Monoclinic form''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | + | Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AGY 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://www.ncbi.nlm.nih.gov/pubmed/16614214 16614214] | 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: Aralkylamine dehydrogenase]] | [[Category: Aralkylamine dehydrogenase]] | ||
| - | [[Category: Protein complex]] | ||
[[Category: Basran, J.]] | [[Category: Basran, J.]] | ||
[[Category: Hothi, P.]] | [[Category: Hothi, P.]] | ||
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[[Category: Scrutton, N S.]] | [[Category: Scrutton, N S.]] | ||
[[Category: Sutcliffe, M J.]] | [[Category: Sutcliffe, M J.]] | ||
| - | [[Category: | + | [[Category: Oxidoreductase]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 19:02:08 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 16:02, 3 May 2008
Crystal structure of the Schiff base intermediate in the reductive half-reaction of aromatic amine dehydrogenase (AADH) with tryptamine. Monoclinic form
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
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 Sat May 3 19:02:08 2008
