2d1w
From Proteopedia
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| - | [[Image:2d1w.png|left|200px]] | ||
| - | + | ==Substrate Schiff-Base intermediate with tyramine in copper amine oxidase from Arthrobacter globiformis== | |
| + | <StructureSection load='2d1w' size='340' side='right'caption='[[2d1w]], [[Resolution|resolution]] 1.74Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2d1w]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arthrobacter_globiformis Arthrobacter globiformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D1W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2D1W 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]] 1.74Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=TTS:3-((3E)-4-HYDROXY-3-{[2-(4-HYDROXYPHENYL)ETHYL]IMINO}-6-OXOCYCLOHEXA-1,4-DIEN-1-YL)ALANINE'>TTS</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=2d1w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d1w OCA], [https://pdbe.org/2d1w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2d1w RCSB], [https://www.ebi.ac.uk/pdbsum/2d1w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2d1w ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/PAOX_ARTGO PAOX_ARTGO] | ||
| + | == 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/d1/2d1w_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=2d1w ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | A key step decisively affecting the catalytic efficiency of copper amine oxidase is stereospecific abstraction of substrate alpha-proton by a conserved Asp residue. We analyzed this step by pre-steady-state kinetics using a bacterial enzyme and stereospecifically deuterium-labeled substrates, 2-phenylethylamine and tyramine. A small and temperature-dependent kinetic isotope effect (KIE) was observed with 2-phenylethylamine, whereas a large and temperature-independent KIE was observed with tyramine in the alpha-proton abstraction step, showing that this step is driven by quantum mechanical hydrogen tunneling rather than the classical transition-state mechanism. Furthermore, an Arrhenius-type preexponential factor ratio approaching a transition-state value was obtained in the reaction of a mutant enzyme lacking the critical Asp. These results provide strong evidence for enzyme-enhanced hydrogen tunneling. X-ray crystallographic structures of the reaction intermediates revealed a small difference in the binding mode of distal parts of substrates, which would modulate hydrogen tunneling proceeding through either active or passive dynamics. | ||
| - | + | Quantum mechanical hydrogen tunneling in bacterial copper amine oxidase reaction.,Murakawa T, Okajima T, Kuroda S, Nakamoto T, Taki M, Yamamoto Y, Hayashi H, Tanizawa K Biochem Biophys Res Commun. 2006 Apr 7;342(2):414-23. Epub 2006 Feb 8. PMID:16487484<ref>PMID:16487484</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 2d1w" style="background-color:#fffaf0;"></div> | |
| - | + | ||
==See Also== | ==See Also== | ||
*[[Copper Amine Oxidase|Copper Amine Oxidase]] | *[[Copper Amine Oxidase|Copper Amine Oxidase]] | ||
| - | + | *[[Copper amine oxidase 3D structures|Copper amine oxidase 3D structures]] | |
| - | == | + | == References == |
| - | < | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Arthrobacter globiformis]] | [[Category: Arthrobacter globiformis]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Hayashi | + | [[Category: Hayashi H]] |
| - | [[Category: Kuroda | + | [[Category: Kuroda S]] |
| - | [[Category: Murakawa | + | [[Category: Murakawa T]] |
| - | [[Category: Nakamoto | + | [[Category: Nakamoto T]] |
| - | [[Category: Okajima | + | [[Category: Okajima T]] |
| - | [[Category: Taki | + | [[Category: Taki M]] |
| - | [[Category: Tanizawa | + | [[Category: Tanizawa K]] |
| - | [[Category: Yamamoto | + | [[Category: Yamamoto Y]] |
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Current revision
Substrate Schiff-Base intermediate with tyramine in copper amine oxidase from Arthrobacter globiformis
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