2agx: Difference between revisions
New page: left|200px<br /><applet load="2agx" size="450" color="white" frame="true" align="right" spinBox="true" caption="2agx, resolution 2.200Å" /> '''Crystal structure o... |
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[[Image:2agx.gif|left|200px]]<br /><applet load="2agx" size=" | [[Image:2agx.gif|left|200px]]<br /><applet load="2agx" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2agx, resolution 2.200Å" /> | caption="2agx, resolution 2.200Å" /> | ||
'''Crystal structure of the Schiff base intermediate in the reductive half-reaction of aromatic amine dehydrogenase (AADH) with tryptamine. P212121 form'''<br /> | '''Crystal structure of the Schiff base intermediate in the reductive half-reaction of aromatic amine dehydrogenase (AADH) with tryptamine. P212121 form'''<br /> | ||
==Overview== | ==Overview== | ||
We present an atomic-level description of the reaction chemistry of an | 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== | ==About this Structure== | ||
2AGX is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Alcaligenes_faecalis Alcaligenes faecalis] with TSH as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http:// | 2AGX is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Alcaligenes_faecalis Alcaligenes faecalis] with <scene name='pdbligand=TSH:'>TSH</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AGX OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Basran, J.]] | [[Category: Basran, J.]] | ||
[[Category: Hothi, P.]] | [[Category: Hothi, P.]] | ||
[[Category: Johannissen, L | [[Category: Johannissen, L O.]] | ||
[[Category: Leys, D.]] | [[Category: Leys, D.]] | ||
[[Category: Masgrau, L.]] | [[Category: Masgrau, L.]] | ||
[[Category: Mulholland, A | [[Category: Mulholland, A J.]] | ||
[[Category: Ranaghan, K | [[Category: Ranaghan, K E.]] | ||
[[Category: Roujeinikova, A.]] | [[Category: Roujeinikova, A.]] | ||
[[Category: Scrutton, N | [[Category: Scrutton, N S.]] | ||
[[Category: Sutcliffe, M | [[Category: Sutcliffe, M J.]] | ||
[[Category: TSH]] | [[Category: TSH]] | ||
[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:27:16 2008'' | ||
Revision as of 17:27, 21 February 2008
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Crystal structure of the Schiff base intermediate in the reductive half-reaction of aromatic amine dehydrogenase (AADH) with tryptamine. P212121 form
OverviewOverview
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 StructureAbout this Structure
2AGX is a Protein complex structure of sequences from Alcaligenes faecalis with as ligand. Active as Aralkylamine dehydrogenase, with EC number 1.4.99.4 Full crystallographic information is available from OCA.
ReferenceReference
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
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