2h47

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[[Image:2h47.gif|left|200px]]
 
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==Crystal Structure of an Electron Transfer Complex Between Aromatic Amine Dephydrogenase and Azurin from Alcaligenes Faecalis (Form 1)==
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The line below this paragraph, containing "STRUCTURE_2h47", creates the "Structure Box" on the page.
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<StructureSection load='2h47' size='340' side='right'caption='[[2h47]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2h47]] is a 9 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=2H47 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H47 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
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<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=TRQ:2-AMINO-3-(6,7-DIOXO-6,7-DIHYDRO-1H-INDOL-3-YL)-PROPIONIC+ACID'>TRQ</scene></td></tr>
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{{STRUCTURE_2h47| PDB=2h47 | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2h47 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h47 OCA], [https://pdbe.org/2h47 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h47 RCSB], [https://www.ebi.ac.uk/pdbsum/2h47 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h47 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h4/2h47_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2h47 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The crystal structure of an electron transfer complex of aromatic amine dehydrogenase (AADH) and azurin is presented. Electrons are transferred from the tryptophan tryptophylquinone (TTQ) cofactor of AADH to the type I copper of the cupredoxin azurin. This structure is compared with the complex of the TTQ-containing methylamine dehydrogenase (MADH) and the cupredoxin amicyanin. Despite significant similarities between the two quinoproteins and the two cupredoxins, each is specific for its respective partner and the ionic strength dependence and magnitude of the binding constant for each complex are quite different. The AADH-azurin interface is largely hydrophobic, covering approximately 500 A(2) of surface on each molecule, with one direct hydrogen bond linking them. The closest distance from TTQ to copper is 12.6 A compared with a distance of 9.3 A in the MADH-amicyanin complex. When the MADH-amicyanin complex is aligned with the AADH-azurin complex, the amicyanin lies on top of the azurin but is oriented quite differently. Although the copper atoms differ in position by approximately 4.7 A, the amicyanin bound to MADH appears to be rotated approximately 90 degrees from its aligned position with azurin. Comparison of the structures of the two complexes identifies features of the interface that dictate the specificity of the protein-protein interaction and determine the rate of interprotein electron transfer.
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'''Crystal Structure of an Electron Transfer Complex Between Aromatic Amine Dephydrogenase and Azurin from Alcaligenes Faecalis (Form 1)'''
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Crystal structure of an electron transfer complex between aromatic amine dehydrogenase and azurin from Alcaligenes faecalis.,Sukumar N, Chen ZW, Ferrari D, Merli A, Rossi GL, Bellamy HD, Chistoserdov A, Davidson VL, Mathews FS Biochemistry. 2006 Nov 14;45(45):13500-10. PMID:17087503<ref>PMID:17087503</ref>
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==Overview==
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The crystal structure of an electron transfer complex of aromatic amine dehydrogenase (AADH) and azurin is presented. Electrons are transferred from the tryptophan tryptophylquinone (TTQ) cofactor of AADH to the type I copper of the cupredoxin azurin. This structure is compared with the complex of the TTQ-containing methylamine dehydrogenase (MADH) and the cupredoxin amicyanin. Despite significant similarities between the two quinoproteins and the two cupredoxins, each is specific for its respective partner and the ionic strength dependence and magnitude of the binding constant for each complex are quite different. The AADH-azurin interface is largely hydrophobic, covering approximately 500 A(2) of surface on each molecule, with one direct hydrogen bond linking them. The closest distance from TTQ to copper is 12.6 A compared with a distance of 9.3 A in the MADH-amicyanin complex. When the MADH-amicyanin complex is aligned with the AADH-azurin complex, the amicyanin lies on top of the azurin but is oriented quite differently. Although the copper atoms differ in position by approximately 4.7 A, the amicyanin bound to MADH appears to be rotated approximately 90 degrees from its aligned position with azurin. Comparison of the structures of the two complexes identifies features of the interface that dictate the specificity of the protein-protein interaction and determine the rate of interprotein electron transfer.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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2H47 is a [[Single protein]] structure of sequence 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=2H47 OCA].
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</div>
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<div class="pdbe-citations 2h47" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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Crystal structure of an electron transfer complex between aromatic amine dehydrogenase and azurin from Alcaligenes faecalis., Sukumar N, Chen ZW, Ferrari D, Merli A, Rossi GL, Bellamy HD, Chistoserdov A, Davidson VL, Mathews FS, Biochemistry. 2006 Nov 14;45(45):13500-10. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17087503 17087503]
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*[[Aromatic amine dehydrogenase 3D structures|Aromatic amine dehydrogenase 3D structures]]
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*[[Azurin 3D structures|Azurin 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Alcaligenes faecalis]]
[[Category: Alcaligenes faecalis]]
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[[Category: Aralkylamine dehydrogenase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Bellamy HD]]
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[[Category: Bellamy, H D.]]
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[[Category: Chen Z]]
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[[Category: Chen, Z.]]
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[[Category: Chistoserdov A]]
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[[Category: Chistoserdov, A.]]
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[[Category: Davidson VL]]
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[[Category: Davidson, V L.]]
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[[Category: Ferrati D]]
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[[Category: Ferrati, D.]]
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[[Category: Leys D]]
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[[Category: Leys, D.]]
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[[Category: Mathews FS]]
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[[Category: Mathews, F S.]]
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[[Category: Merli A]]
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[[Category: Merli, A.]]
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[[Category: Rossi GL]]
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[[Category: Rossi, G L.]]
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[[Category: Scrutton NS]]
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[[Category: Scrutton, N S.]]
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[[Category: Sukumar N]]
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[[Category: Sukumar, N.]]
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[[Category: Cupredoxin]]
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[[Category: Electron transfer]]
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[[Category: Quinoprotein]]
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[[Category: Tryptophan tryptophylquinone]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 05:50:51 2008''
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Current revision

Crystal Structure of an Electron Transfer Complex Between Aromatic Amine Dephydrogenase and Azurin from Alcaligenes Faecalis (Form 1)

PDB ID 2h47

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