2agz: Difference between revisions

Revision as of 05:18, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2agz.png

Template:STRUCTURE 2agz

Crystal structure of the carbinolamine intermediate in the reductive half-reaction of aromatic amine dehydrogenase (AADH) with tryptamine. F222 formCrystal structure of the carbinolamine intermediate in the reductive half-reaction of aromatic amine dehydrogenase (AADH) with tryptamine. F222 form

Template:ABSTRACT PUBMED 16614214

About this StructureAbout this Structure

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

Page seeded by OCA on Tue Jul 29 05:18:44 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:2agz.gif|left|200px]]
+{{Seed}}
+[[Image:2agz.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_2agz|  PDB=2agz  |  SCENE=  }}
-'''Crystal structure of the carbinolamine intermediate in the reductive half-reaction of aromatic amine dehydrogenase (AADH) with tryptamine. F222 form'''
+===Crystal structure of the carbinolamine intermediate in the reductive half-reaction of aromatic amine dehydrogenase (AADH) with tryptamine. F222 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.
+The line below this paragraph, {{ABSTRACT_PUBMED_16614214}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16614214 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16614214}}
 ==About this Structure==
@@ Line 32: / Line 36: @@
 [[Category: Sutcliffe, M J.]]
 [[Category: Oxidoreductase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 19:02:10 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 05:18:44 2008''