2agz: Difference between revisions

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-[[Image:2agz.gif|left|200px]]
-<!--
-The line below this paragraph, containing "STRUCTURE_2agz", creates the "Structure Box" on the page.
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-or leave the SCENE parameter empty for the default display.
--->
-{{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==
+<StructureSection load='2agz' size='340' side='right'caption='[[2agz]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2agz]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Alcaligenes_faecalis Alcaligenes faecalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AGZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AGZ FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TRQ:2-AMINO-3-(6,7-DIOXO-6,7-DIHYDRO-1H-INDOL-3-YL)-PROPIONIC+ACID'>TRQ</scene>, <scene name='pdbligand=TSC:(1S)-1-AMINO-2-(1H-INDOL-3-YL)ETHANOL'>TSC</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2agz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2agz OCA], [https://pdbe.org/2agz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2agz RCSB], [https://www.ebi.ac.uk/pdbsum/2agz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2agz ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/AAUA_ALCFA AAUA_ALCFA] Oxidizes primary aromatic amines and, more slowly, some long-chain aliphatic amines, but not methylamine or ethylamine. Uses azurin as an electron acceptor to transfer electrons from the reduced tryptophylquinone cofactor.<ref>PMID:11495996</ref> <ref>PMID:16279953</ref> <ref>PMID:8188594</ref> <ref>PMID:7876189</ref> <ref>PMID:17087503</ref> <ref>PMID:17005560</ref> <ref>PMID:16614214</ref>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ag/2agz_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2agz ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-==Overview==
+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<ref>PMID:16614214</ref>
-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==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AGZ OCA].
+</div>
+<div class="pdbe-citations 2agz" style="background-color:#fffaf0;"></div>
-==Reference==
+==See Also==
-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]
+*[[Aromatic amine dehydrogenase 3D structures|Aromatic amine dehydrogenase 3D structures]]
-[[Category: Aralkylamine dehydrogenase]]
+== References ==
-[[Category: Basran, J.]]
+<references/>
-[[Category: Hothi, P.]]
+__TOC__
-[[Category: Johannissen, L O.]]
+</StructureSection>
-[[Category: Leys, D.]]
+[[Category: Alcaligenes faecalis]]
-[[Category: Masgrau, L.]]
+[[Category: Large Structures]]
-[[Category: Mulholland, A J.]]
+[[Category: Basran J]]
-[[Category: Ranaghan, K E.]]
+[[Category: Hothi P]]
-[[Category: Roujeinikova, A.]]
+[[Category: Johannissen LO]]
-[[Category: Scrutton, N S.]]
+[[Category: Leys D]]
-[[Category: Sutcliffe, M J.]]
+[[Category: Masgrau L]]
-[[Category: Oxidoreductase]]
+[[Category: Mulholland AJ]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 19:02:10 2008''
+[[Category: Ranaghan KE]]
+[[Category: Roujeinikova A]]
+[[Category: Scrutton NS]]
+[[Category: Sutcliffe MJ]]