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- | [[Image:2agl.gif|left|200px]] | |
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- | {{Structure
| + | ==Crystal structure of the phenylhydrazine adduct of aromatic amine dehydrogenase from Alcaligenes faecalis== |
- | |PDB= 2agl |SIZE=350|CAPTION= <scene name='initialview01'>2agl</scene>, resolution 1.400Å
| + | <StructureSection load='2agl' size='340' side='right'caption='[[2agl]], [[Resolution|resolution]] 1.40Å' scene=''> |
- | |SITE=
| + | == Structural highlights == |
- | |LIGAND= <scene name='pdbligand=PHZ:1-PHENYLHYDRAZINE'>PHZ</scene>, <scene name='pdbligand=TRQ:2-AMINO-3-(6,7-DIOXO-6,7-DIHYDRO-1H-INDOL-3-YL)-PROPIONIC+ACID'>TRQ</scene> | + | <table><tr><td colspan='2'>[[2agl]] 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=2AGL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AGL FirstGlance]. <br> |
- | |ACTIVITY= <span class='plainlinks'>[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] </span>
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4Å</td></tr> |
- | |GENE=
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PHZ:1-PHENYLHYDRAZINE'>PHZ</scene>, <scene name='pdbligand=TRQ:2-AMINO-3-(6,7-DIOXO-6,7-DIHYDRO-1H-INDOL-3-YL)-PROPIONIC+ACID'>TRQ</scene></td></tr> |
- | |DOMAIN=
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2agl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2agl OCA], [https://pdbe.org/2agl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2agl RCSB], [https://www.ebi.ac.uk/pdbsum/2agl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2agl ProSAT]</span></td></tr> |
- | |RELATEDENTRY=[[2agu|2AGU]], [[2agw|2AGW]], [[2agx|2AGX]], [[2agy|2AGY]], [[2agz|2AGZ]], [[2ah0|2AH0]], [[2ah1|2AH1]]
| + | </table> |
- | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2agl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2agl OCA], [http://www.ebi.ac.uk/pdbsum/2agl PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2agl RCSB]</span>
| + | == 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/2agl_consurf.spt"</scriptWhenChecked> |
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=2agl ConSurf]. |
| + | <div style="clear:both"></div> |
| | | |
- | '''Crystal structure of the phenylhydrazine adduct of aromatic amine dehydrogenase from Alcaligenes faecalis'''
| + | ==See Also== |
- | | + | *[[Aromatic amine dehydrogenase 3D structures|Aromatic amine dehydrogenase 3D structures]] |
- | | + | == References == |
- | ==Overview== | + | <references/> |
- | 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.
| + | __TOC__ |
- | | + | </StructureSection> |
- | ==About this Structure== | + | |
- | 2AGL is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Alcaligenes_faecalis Alcaligenes faecalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AGL OCA].
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- | | + | |
- | ==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]
| + | |
| [[Category: Alcaligenes faecalis]] | | [[Category: Alcaligenes faecalis]] |
- | [[Category: Aralkylamine dehydrogenase]] | + | [[Category: Large Structures]] |
- | [[Category: Protein complex]]
| + | [[Category: Basran J]] |
- | [[Category: Basran, J.]] | + | [[Category: Hothi P]] |
- | [[Category: Hothi, P.]] | + | [[Category: Johannissen LO]] |
- | [[Category: Johannissen, L O.]] | + | [[Category: Leys D]] |
- | [[Category: Leys, D.]] | + | [[Category: Masgrau L]] |
- | [[Category: Masgrau, L.]] | + | [[Category: Mulholland AJ]] |
- | [[Category: Mulholland, A J.]] | + | [[Category: Ranaghan KE]] |
- | [[Category: Ranaghan, K E.]] | + | [[Category: Roujeinikova A]] |
- | [[Category: Roujeinikova, A.]] | + | [[Category: Scrutton NS]] |
- | [[Category: Scrutton, N S.]] | + | [[Category: Sutcliffe MJ]] |
- | [[Category: Sutcliffe, M J.]] | + | |
- | [[Category: oxidoreductase]]
| + | |
- | | + | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:52:25 2008''
| + | |
| Structural highlights
Function
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.[1] [2] [3] [4] [5] [6] [7]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
See Also
References
- ↑ Chistoserdov AY. Cloning, sequencing and mutagenesis of the genes for aromatic amine dehydrogenase from Alcaligenes faecalis and evolution of amine dehydrogenases. Microbiology. 2001 Aug;147(Pt 8):2195-202. PMID:11495996
- ↑ Hothi P, Khadra KA, Combe JP, Leys D, Scrutton NS. Tryptophan tryptophylquinone cofactor biogenesis in the aromatic amine dehydrogenase of Alcaligenes faecalis. Cofactor assembly and catalytic properties of recombinant enzyme expressed in Paracoccus denitrificans. FEBS J. 2005 Nov;272(22):5894-909. PMID:16279953 doi:http://dx.doi.org/EJB4990
- ↑ Govindaraj S, Eisenstein E, Jones LH, Sanders-Loehr J, Chistoserdov AY, Davidson VL, Edwards SL. Aromatic amine dehydrogenase, a second tryptophan tryptophylquinone enzyme. J Bacteriol. 1994 May;176(10):2922-9. PMID:8188594
- ↑ Edwards SL, Davidson VL, Hyun YL, Wingfield PT. Spectroscopic evidence for a common electron transfer pathway for two tryptophan tryptophylquinone enzymes. J Biol Chem. 1995 Mar 3;270(9):4293-8. PMID:7876189
- ↑ Sukumar N, Chen ZW, Ferrari D, Merli A, Rossi GL, Bellamy HD, Chistoserdov A, Davidson VL, Mathews FS. Crystal structure of an electron transfer complex between aromatic amine dehydrogenase and azurin from Alcaligenes faecalis. Biochemistry. 2006 Nov 14;45(45):13500-10. PMID:17087503 doi:http://dx.doi.org/10.1021/bi0612972
- ↑ Roujeinikova A, Scrutton NS, Leys D. Atomic level insight into the oxidative half-reaction of aromatic amine dehydrogenase. J Biol Chem. 2006 Dec 29;281(52):40264-72. Epub 2006 Sep 27. PMID:17005560 doi:http://dx.doi.org/10.1074/jbc.M605559200
- ↑ Masgrau L, Roujeinikova A, Johannissen LO, Hothi P, Basran J, Ranaghan KE, Mulholland AJ, Sutcliffe MJ, Scrutton NS, Leys D. Atomic description of an enzyme reaction dominated by proton tunneling. Science. 2006 Apr 14;312(5771):237-41. PMID:16614214 doi:312/5771/237
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